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PubMed2002

Lack of simian immunodeficiency virus (SIV) specific IgA response in the intestine of SIV infected rhesus macaques.

BACKGROUND: Little is known about secretory immunity-the major defence mechanism at mucosal surfaces-in human immunodeficiency virus (HIV) infected patients, especially in the early stages of the disease. AIMS: The aim of the study was to analyse mucosal immunoglobulin production and simian immunodeficiency virus (SIV) specific antibody response in the intestinal mucosa during the course of SIV infection in comparison with serum and saliva. ANIMALS AND METHODS: IgG, IgA, and IgM concentrations were determined in supernatants of short term cultured duodenal biopsies, serum, and saliva from SIV infected rhesus macaques (n=8) and controls (n=2) by ELISA at defined times before and after infection. Specific antibodies to SIV were detected by western blot and/or dot blot analysis. In addition, rectal swabs from two uninfected and 12 SIV infected rhesus macaques (seven without and five with enteritis) were analysed for albumin and IgG concentrations. RESULTS: An increase in total intestinal IgG and a decrease in IgA were observed. SIV specific IgG or IgA responses were detectable as early as one week after SIV infection in the serum of seven of eight animals. In contrast, intestinal SIV specific IgG production was detected only four weeks after infection in six of eight animals, and intestinal SIV specific IgA was not produced in the intestine at any time point. In saliva, the secretory component on SIV specific IgA was only detected in one animal at week 24 after infection. Enteritis is frequent in SIV infected animals and results in a significant increase in albumin and IgG secretion into the intestinal lumen. CONCLUSION: Despite modest quantitative changes in mucosal immunglobulin production there was a total lack of SIV specific IgA synthesis in the intestine during SIV infection. This lack or disturbed secretory SIV specific IgA response at mucosal surfaces may explain the rapid and high HIV/SIV replication in this compartment. In addition, our investigations indicate secretion of serum proteins into intestinal fluids during SIV infection. Previous investigations using intestinal secretions or swabs for analysing quantitative and specific immunglobulins therefore should be interpreted with caution.

Animals↗
PubMed1997

Relationship between interdigestive motility and secretion of immunoglobulin A in human proximal small intestine.

In 17 healthy volunteers, we studied the dynamics of secretory immunoglobulin A (SIgA) release in the proximal small intestine (distal duodenum and proximal jejunum), using a modified triple-lumen perfusion technique. Secretory data were related to the current phase of the migrating motor complex (MMC), as recorded by manometry. In both segments, luminal SIgA output changed cyclically, with peak outputs occurring at the end of the MMC cycle (late phase II). These MMC-related changes were due to two factors: cyclic inflow of SIgA from more proximal sites, and a cyclic release of SIgA from the test segment that correlated in time with an increase in epithelial fluid secretion. Cyclic intestinal SIgA release may thus be another secretory component of the MMC. The data are compatible with the hypothesis that motility and SIgA release are linked by motility-activated chloride secretion from the intestinal crypts.

Adult↗
PubMedDate not supplied

[Obtention of monoclonal antibodies against human secretory IgA].

In order to determine the IgA levels in secretions, the authors engaged themselves to obtain monoclonal antibodies against this immunoglobulin and to show their possible utilization in the development of quantitation methods. 6 monoclonal antibodies were obtained: one against the secretory component (SC) and five against the heavy-chain (HC) of IgA. IgA purified from human colostrum was used as immunogen (HC). The immunoglobulin isotypes (IgG2a and IgG1) were determined in 2 monoclonal antibodies, one against SC and the other against HC. Polyacrylamide gel electrophoresis was performed in the presence of sodium dodecyl sulphate and b-mercapto-ethanol. Immunotransference was also carried out to determine their specificity. Secretory IgA was detected in saliva specimens. The anti-SC monoclonal antibody obtained in-the laboratory of the "Pedro Kourí" Institute of Tropical Medicine (IPK) was compared with a commercial one (Sigma Chemical Co.), and a similar behaviour was observed. The monoclonal antibody against SC (IPK) was used to detect IgA specific to LPS ogawa in persons vaccinated with an attenuated strain of Vibrio cholerae. Marked differences were found between the levels before and after immunization. The anti-HC monoclonal antibody was utilized to make an ELISA-like simulated system. The detection limit was 9.89 ng/mL.

Antibodies, Monoclonal↗
PubMed1984

Immunoelectronmicroscopic study on the transport of secretory IgA in the lower respiratory tract and alveoli.

To define the immunocytochemical localization of secretory component (SC), IgA and J chain in human bronchioles and alveoli, a direct peroxidase-labeled antibody method was used. SC was found in non-ciliated cells of the bronchioles including respiratory bronchioles and type II alveolar epithelial cells, whereas SC was rarely present in ciliated cells and type I alveolar epithelial cells and was absent from goblet cells. In the positively reacting cells, SC was found in secretory protein synthetic organelles such as perinuclear spaces and endoplasmic reticulum, Golgi complexes, and on the external surfaces of the apical and basolateral plasma membranes. IgA and J chain were localized in the epithelial cells where SC was found. Ultrastructually IgA was present on the apical and basolateral plasma membranes, in pinocytic invaginations of the membranes, and in vesicles distributed through the cytoplasm, especially in the apical cytoplasm of the epithelial cells where SC was found. In addition, IgA and J chain were found to be associated with the endothelial cells of the capillaries, plasma cells and the surrounding interstitium. These observations suggest that SC is synthesized and secreted by epithelial cells, especially non-ciliated cells of the bronchioles including respiratory bronchioles and type II alveolar epithelial cells. They also suggest that secretory IgA (sIgA) is transported into alveolar spaces and the bronchiolar lumen through these cells by SC-mediated transport mechanism. This sIgA may play an important role in defense mechanisms of the lower respiratory tract and alveoli.

Biological Transport↗
PubMed1988

An immunohistochemical study of pleomorphic adenomas of the salivary gland: glial fibrillary acidic protein-like immunoreactivity identifies a major myoepithelial component.

An immunohistochemical study of 34 pleomorphic adenomas of the major salivary glands demonstrated phenotypic differences among the various morphologic regions in these tumors. The phenotypes expressed were comparable to those of normal salivary gland cells. In the normal glands, myoepithelial cells were immunoreactive for glial fibrillary acidic protein (GFAP), S-100 protein, and keratin; acinic cells exhibited strong, predominantly nuclear S-100 staining and weaker keratin staining; intercalated ducts had both cytoplasmic and nuclear S-100 positivity; and several epithelial antigens were observed throughout the ductal system. In the tumors, the presence of classic epithelial markers (including carcinoembryonic antigen, epithelial membrane antigen, secretory component, and keratin) in the luminal cells of ducts and the intense immunoreactivity with GFAP (with weaker keratin and S-100 staining) in periductal and stromal cells indicated distinct epithelial and myoepithelial differentiation. Solid epithelioid areas consisted phenotypically of intercalated duct/acinic cells and/or myoepithelial cells, the former exhibiting predominant nuclear S-100 positivity. The presence of GFAP-like immunoreactivity in normal myoepithelial cells strongly supports the extensive involvement of this cell in pleomorphic adenomas. The spectrum of phenotypes expressed adds weight to existing evidence for pleomorphism rather than a mixed origin of this tumor. The combination of keratin, S-100, and GFAP immunostaining is particularly useful in identifying the component cells in pleomorphic adenomas of the salivary glands.

Adenoma↗
PubMed1978

Localization of the effect of acetylcholine in regulating intestinal ion transport.

1. The location of the site involved in the secretory response of rat jejunum and colon to ACh was investigated by selectively damaging either the villi of the jejunum and the surface epithelium of the colon or the crypts. 2. The secretory response induced by ACh was measured both in terms of changes in electrical activity and chloride fluxes. 3. Exposure of the mucosa to 2 M-Na2SO4 for 30 min selectively damaged the jejunal villi and colonic surface epithelium but did not reduce the increased potential difference and current generated by ACh. 4. When resistance changes were taken into account the colonic response was markedly increased after Na2SO4 treatment although the jejunal response was unchanged. Under control conditions ACh reduced net Na absorption and stimulated Cl secretion by the colon. After exposure to Na2SO4 only the Cl secretory component of the ACh response remained, thus accounting for the enhanced effect. 5. Cycloheximide, administered I.V. at a dose of 12 mg/kg, damaged the crypts after 2 hr without affecting the villi of the jejunum or the surface epithelium of the colon. After cycloheximide treatment the increased potential difference, current and net Cl secretion induced by ACh were significantly reduced. 6. The crypts therefore appear to be the site primarily involved in the secretory response of rat jejunum and colon to ACh, although in the colon an inhibitory effect on the Na transport process located in the surface epithelium was observed.

Acetylcholine↗
PubMed2001

Investigation of the role of prolactin in the development and function of the lacrimal and harderian glands using genetically modified mice.

PURPOSE: To determine whether prolactin receptor is essential for normal development and function of the lacrimal gland and whether hyperprolactinemia can alter lacrimal development. METHODS: Lacrimal gland morphology and function were examined in two genetic mouse models of prolactin action: a prolactin receptor knockout model that is devoid of prolactin action and a transgenic model of hyperprolactinemia. RESULTS: Image analysis of lacrimal and Harderian gland sections was used to quantify glandular morphology. In females, lacrimal acinar area decreased by 30% and acinar cell density increased by 25% over control subjects in prolactin transgenic animals, but prolactin receptor knockout mice showed no changes. In males, transgenic animals showed no changes, but prolactin receptor knockout mice showed a 5% reduction in acinar area and an 11% increase in acinar cell density, which was lost after castration. The morphology of the Harderian glands underwent parallel changes but to a lesser degree. A complete loss of porphyrin accretions was seen in the Harderian glands of male and female knockout animals. No differences in tear protein levels were seen in knockout animals by two-dimensional gels. Enzyme-linked immunosorbent assay (ELISA) and Western blot analysis showed that the level of secretory component and IgA in knockout mouse tears remained unchanged. There was no change in the predisposition of the 129 mouse strain to conjunctivitis in the knockout animals. CONCLUSIONS: Prolactin plays a small role in establishing the sexual dimorphism of male lacrimal glands. In females, hyperprolactinemia causes a hyperfemale morphology, suggesting a role in dry eye syndromes. Prolactin is required for porphyrin secretion by the Harderian gland but plays no essential role in the secretory immune function of the lacrimal gland.

Animals↗
PubMed1988

Biochemistry and lectin binding properties of mammalian salivary mucous glycoproteins.

The molecules responsible for the highly viscous properties of mucus are secretory glycoproteins referred to as mucins. Salivary mucins are characterized by a high sugar to protein ratio and are of a broad range of molecular weight from 7 x 10(4) to millions. With a few exceptions, they contain up to 30% of hexosamine (galactosamine and glucosamine), 8-33% of sialic acid, trace to 15% of galactose or fucose and little or no mannose. The size of carbohydrate side chains of these glycoproteins ranges from one to about fifteen units of sugar. These carbohydrate side chains are usually O-glycosidically linked through N-acetylgalactosamine to a peptidyl serine or threonine. In some instances, ester sulfate groups, mainly on N-acetylglucosamine, are also a structural feature. In many of these glycoproteins, the saccharide sequence is the same as that which determines the specificity of blood groups. Carbohydrate sequence analysis shows that salivary mucins exhibit considerable polydispersity, great diversity and remarkable structural flexibility not only among animal species but also within the same mucin molecule. Based on their lectin-binding ability, they can be used for purification of lectins, and lectins coupled to resin may be useful for the isolation of mucin-type glycoproteins. The epithelial mucous secretions modulate oral microbial flora; many secretory components serve as lectin-receptors for the attachment of microbes. The judicious use of lectins with widely differing binding characteristics has already been valuable in the in situ localization of salivary glycoproteins, in elucidating structural details, recording sugar density within a given tissue section, and defining host-parasite interactions. It is hoped that their use, together with monoclonal antibody (158) and tissue culture techniques (159, 160) will further clarify the roles of individual secretory mucous glycoproteins in health and disease.

Animals↗
PubMed1998

Intestinal handling of mercury in the rat: implications of intestinal secretion of inorganic mercury following biliary ligation or cannulation.

Three sets of experiments were carried out to determine if there is an intestinal secretory component in the fecal excretion of administered inorganic mercury. In the first set of experiments the disposition of a nontoxic 0.5-micromol/kg intravenous dose of inorganic mercury was evaluated in control rats and rats whose bile duct had been ligated. Data collected 24 h after the administration of mercuric chloride indicated that some inorganic mercury had moved from the blood across the epithelium into the lumen of the stomach, small intestine, and large intestine. This secretory movement of mercury was most prominent in the small intestine. Interestingly, the renal uptake and accumulation of mercury were diminished significantly in the rats whose bile duct had been ligated. A time-course experiment showed that the maximum amount of secretory movement of mercury into the lumen of the small intestine occurred during the initial 12 h after the injection of mercuric chloride. By the end of 24 h after the injection of mercuric chloride, much of the inorganic mercury secreted in the small intestine appeared to have moved down into the large intestine. In a third experiment, the disposition of mercury was evaluated in control rats and rats who had their bile duct cannulated. The rationale for this third experiment was to study the disposition of mercury under conditions where obstruction of biliary outflow from the liver would not be as much of an issue as with ligation of the bile duct. Evidence for movement of mercury into the lumen of the intestines was also obtained from the rats whose bile duct had been ligated. Eighteen hours after the injection of mercuric chloride the amount of mercury in the luminal compartment of the small intestine was not statistically different between the two groups of rats. Approximately 1.7-2.1% of the administered dose was present in the luminal contents of the small intestine. Decreased renal uptake of mercury was also detected in the rats whose bile duct had been cannulated. The findings from the present study show that when bile flow is obstructed or diverted, clear evidence for secretory movement of mercury into the lumen of the gastrointestinal (GI) tract can be demonstrated. These findings also indicate that the secretory movement of mercury into the lumen of the GI tract is a mechanism that contributes significantly to the pool of mercury that is excreted in the feces.

Animals↗
PubMed2001

Quantitative ER <--> Golgi transport kinetics and protein separation upon Golgi exit revealed by vesicular integral membrane protein 36 dynamics in live cells.

To quantitatively investigate the trafficking of the transmembrane lectin VIP36 and its relation to cargo-containing transport carriers (TCs), we analyzed a C-terminal fluorescent-protein (FP) fusion, VIP36-SP-FP. When expressed at moderate levels, VIP36-SP-FP localized to the endoplasmic reticulum, Golgi apparatus, and intermediate transport structures, and colocalized with epitope-tagged VIP36. Temperature shift and pharmacological experiments indicated VIP36-SP-FP recycled in the early secretory pathway, exhibiting trafficking representative of a class of transmembrane cargo receptors, including the closely related lectin ERGIC53. VIP36-SP-FP trafficking structures comprised tubules and globular elements, which translocated in a saltatory manner. Simultaneous visualization of anterograde secretory cargo and VIP36-SP-FP indicated that the globular structures were pre-Golgi carriers, and that VIP36-SP-FP segregated from cargo within the Golgi and was not included in post-Golgi TCs. Organelle-specific bleach experiments directly measured the exchange of VIP36-SP-FP between the Golgi and endoplasmic reticulum (ER). Fitting a two-compartment model to the recovery data predicted first order rate constants of 1.22 +/- 0.44%/min for ER --> Golgi, and 7.68 +/- 1.94%/min for Golgi --> ER transport, revealing a half-time of 113 +/- 70 min for leaving the ER and 1.67 +/- 0.45 min for leaving the Golgi, and accounting for the measured steady-state distribution of VIP36-SP-FP (13% Golgi/87% ER). Perturbing transport with AlF(4)(-) treatment altered VIP36-SP-GFP distribution and changed the rate constants. The parameters of the model suggest that relatively small differences in the first order rate constants, perhaps manifested in subtle differences in the tendency to enter distinct TCs, result in large differences in the steady-state localization of secretory components.

Animals↗
PubMed2001

Lacrimal drainage-associated lymphoid tissue (LDALT): a part of the human mucosal immune system.

PURPOSE: Mucosa-associated lymphoid tissue (MALT) specifically protects mucosal surfaces. In a previous study of the human conjunctiva, evidence was also found for the presence of MALT in the lacrimal sac. The present study, therefore, aims to investigate its morphology and topographical distribution in the human lacrimal drainage system. METHODS: Lacrimal drainage systems (n = 51) obtained from human cadavers were investigated by clearing flat wholemounts or by serial sections of tissue embedded in paraffin, OCT compound, or epoxy resin. These were further analyzed by histology, immunohistochemistry, and electron microscopy. RESULTS: All specimens showed the presence of lymphocytes and plasma cells as a diffuse lymphoid tissue in the lamina propria, together with intraepithelial lymphocytes and occasional high endothelial venules (HEV). It formed a narrow layer along the canaliculi that became thicker in the cavernous parts. The majority of lymphocytes were T cells, whereas B cells were interspersed individually or formed follicular centers. T cells were positive for CD8 and the human mucosa lymphocyte antigen (HML-1). Most plasma cells were positive for IgA and the overlying epithelium expressed its transporter molecule secretory component (SC). Basal mucous glands were present in the lacrimal canaliculi and in the other parts accompanied by alveolar and acinar glands, all producing IgA-rich secretions. Primary and secondary lymphoid follicles possessing HEV were present in about half of the specimens. CONCLUSIONS: The term lacrimal drainage-associated lymphoid tissue (LDALT) is proposed here to describe the lymphoid tissue that is regularly present and belongs to the common mucosal immune system and to the secretory immune system. It is suggested that it may form a functional unit together with the lacrimal gland and conjunctiva, connected by tear flow, lymphocyte recirculation, and probably the neural reflex arc, and play a major role in preserving ocular surface integrity.

Aged↗
PubMed1988

Pathophysiology of rhinitis. 1. Assessment of the sources of protein in methacholine-induced nasal secretions.

Nasal provocation tests with normal saline and methacholine (MC) were performed in 25 atopic and 27 nonatopic subjects in an effort to assess the sources of protein in induced airway secretions. Nasal lavages obtained at baseline and after provocation were analyzed for albumin, total protein, secretory IgA (sIgA), and total IgA. Compared with baseline levels or saline provocation, MC provocation increased the secretion of albumin (p less than 0.025), total protein (p less than 0.001), sIgA (p less than 0.025), and total IgA (p less than 0.025), but did not significantly affect the relative proportions of albumin-to-total protein (albumin percent) or sIgA-to-total IgA (sIgA/total IgA ratio). Nasal pretreatment with atropine significantly inhibited MC-induced secretion of all 4 proteins, again without affecting the albumin percent or the sIgA/total IgA ratio. Because MC is known to stimulate atropine-inhibitable secretion of glandular products, these data suggest that sIgA and albumin may accompany glandular secretions. Immunohistochemical analyses of nasal turbinates confirmed that secretory component was found only on serous cells within submucous glands. Thus, it appears that cholinergic stimulation may regulate sIgA secretion and thereby participate in local nasal (and possibly respiratory tract) immunity.

Adolescent↗
PubMed1983

[Secretory immunoglobulin A in the amniotic fluid of healthy pregnant females].

Amniotic fluid levels of secretory immunoglobulin A (S-AgA) were measured by simple radial immunodiffusion according to the method of Mancini using a monospecific antiserum against the human secretory component. 256 samples from healthy pregnant women were examined. Amniotic fluid S-IgA concentration increases significantly during normal pregnancy and shows a loose correlation to the phospholipid level.

Amniotic Fluid↗
PubMed1975

Antibody response in the parotid fluid and serum of Irus monkeys (Macaca fascicularis) after local immunization with Streptococcus mutans.

The antibody response of Macaca fascicularis in parotid saliva and serum to local immunization by two routes with Streptococcus mutans was studied and compared over 1 year. Antibodies were titrated and classified by indirect immunofluorescent staining using specific antiglobulin conjugates. Antiglucosyltransferase activity was assayed by an enzyme inhibition test. Animals were immunized first by injecting formalin-killed bacterial cells and cell products subcutaneously into the vicinity of the four major salivary glands. The monkeys were next immunized by retrograde instillation of antigen into the parotid duct. Extensive subcutaneous local immunization gave a serum response only. After parotid duct immunization, high titers of immunoglobulin A (IgA) antibody, along with traces of immunoglobulin G (IgG) immunoglobulin M (IgM) antibody, appeared in the parotid saliva, and in the serum high titers of IgG antibody were present along with lower titers of IgA and IgM. IgA antibodies in parotid fluid were shown by double immunofluorescent staining to be associated with antigenic determinants which cross-reacted with an antiserum directed to human secretory component. Titers in parotid fluids and sera fell sharply when immunization was stopped. This response pattern was reproducible. High concentrations of antibody capable of inhibiting glucosyltransferase prepared from S. mutans were found in the sera, but relatively little was detected in the parotid fluids. Extensive immunization via the parotid duct resulted in transient functional impairment of the gland, as evidenced by diminished salivary flow rates. We conclude that parotid ductal immunization can be an effective method for stimulating a salivary secretory IgA antibacterial antibody response.

Administration, Oral↗
PubMed1982

Influence of molecular size of IgA on its immunoassay by various techniques. III. Immunonephelometry.

The influence of size heterogeneity of IgA on its immunonephelometric (IN) assay was studied using highly purified preparations of monoclonal (MC) or polyclonal (PC) monomeric (M), dimeric (D), trimeric (T) and tetrameric (Q) IgA, as well as of secretory IgA (sIgA). Concentrations measured by optical density (OD) were compared to IN--concentrations obtained by using M as standards, on an equal weight basis. No significant difference was found between OD and IN concentrations of D, T, Q and sIgA were only slightly underestimated, with correction factors (CF) of 1.16, 1.20 and 1.24, respectively. The value of 1.24 for our sIgA sample (84% of 11S, 16% of 15S) could be due to the fact that secretory component represents about 20% of the mass of the sIgA molecule. IN seems a method of choice for measuring IgA concentrations in the range of microgram/ml, almost independently of the size of IgA.

Animals↗
PubMed1977

Characterization of the IgA immunocyte population and its product in a patient with excessive intestinal formation of IgA.

An 11-year-old Norwegian boy presented with clinico-pathological features indicative of coeliac or alpha-chain disease. However, his major serum component (about 50 mg/ml) was found to be a polyclonal, polymeric (about 80% dimeric) IgA consisting mainly of the subclass IgA1 and showing a kappa:lambda ratio of 67:33. Also the serum concentration of IgA monomers was increased (about 9 mg/ml). The polymers were heterogeneous with regard to J-chain content--varying on a molar basis from 1.9 for the more basic fraction to at least 2.4 for the more acidic one. Both fractions showed non-covalent affinity for secretory component (SC) in vitro. Most of the serum IgA seemed to originate from the small intestine, which contained a five-times-increased population of IgA immunocytes. These cells were heterogeneous with regard to production of polymeric IgA; many of them showed definitely more J-chain synthesis than normal intestinal IgA immunocytes. The cell population had apparently not spread to the bone marrow, but the polymeric IgA product permeated the connective tissue throughout the body and appeared also in the urine, partly associated with SC. The possibility that such an excessively proliferating intestinal B-cell population may bear some relation to alpha-chain disease is discussed.

B-Lymphocytes↗
PubMed1973

Immunoglobulins of the middle ear fluid in acute otitis media: relationship to serum immunoglobulin concentrations and bacterial cultures.

Immunoglobulin concentrations were studied in 255 specimens of middle ear fluid (MEF) from 165 episodes of acute otitis media in children. There were significant amounts of all three major immunoglobulins (Ig) in MEF, the mean concentration of IgA being 39 mg/100 ml, of IgM 63 mg/100 ml, and of IgG 383 mg/100 ml. Secretory component was present in all 10 MEF specimens in which it was sought. In patients over 9 months of age, there was a decreased likelihood of isolating pathogenic bacteria from MEF if the patient had higher concentrations of IgA in MEF than in simultaneously obtained serum. IgA concentrations were greater in MEF than in serum in almost half the patients, and the mean MEF-serum ratio for IgA was 1.38. Thus, it would appear that in this disorder MEF represents primarily a secretory response to inflammation rather than a transudate.

Animals↗
PubMed1995

Early appearance of antibodies to simian immunodeficiency virus in saliva and serum of infected macaques.

Simian immunodeficiency virus (SIV) infection in macaques is an important animal model for human immunodeficiency virus infection in humans. This study evaluated the temporal development of antibodies to SIV in the parotid saliva of macaques inoculated with the virus and compared these findings with the development of antibodies to SIV in the animals' sera. Three animals (ages, 14, 18, and 18 years) were inoculated with the macrophagetropic strain SIVmac239. Prior to inoculation and at consecutive weekly intervals during a four-week period following the initial virus inoculations, parotid saliva and serum were collected from each animal. A fourth animal (age, 9 years) served as a negative control, and the fifth and sixth animals (ages, 2 and 22 years) served as positive controls (6 and 18 months postinoculation, respectively) with SIVmac239. Saliva and serum samples were reacted against SIV antigen in Western blots (immunoblots) prepared in the standard fashion to determine the presence of antibodies. The reactions of these antigen-antibody complexes with biotinylated anti-human immunoglobulin A (IgA), IgM, and IgG and biotinylated anti-human secretory component (SC) determined the class of antibody present or the presence of SC in the original parotid saliva or serum samples. In infected animals, the IgM to SIV was detectable in serum and saliva at 13 days, and antiviral IgA and IgG in serum and saliva were detectable at 20 to 27 days postinoculation. The antibody to SC reacted to saliva from only two animals at 20 and 27 days, and long-term positive controls were positive for SC in saliva, indicating that either secretory IgA or secretory IgM was present in these samples. Antibodies to SIVmac239 antigens have therefore been detected in saliva as early as 13 days postinfection. Saliva may be as useful as serum as a diagnostic specimen and/or disease-monitoring method in this important animal model.

Animals↗