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PubMed1996

Chicken Mhc alloantiserum cross-reactivity analysis by hemagglutination and flow cytometry.

The major histocompatibility complex (Mhc) haplotype in the chicken is generally determined by the use of alloantisera in a hemagglutination assay. This method restricts haplotype determination to antigens expressed on the surface of erythrocytes which includes class I (B - F) and class IV (B - G) antigens as well as any other polymorphic molecules on these cells. Alloantisera can result in complex cross-reactivity patterns. We describe here the analysis of 53 alloantisera made within Mhc-congenic lines. Each antiserum was tested by hemagglutination with erythrocytes and by flow cytometry with erythrocytes and peripheral white blood cells of seven Mhc haplotypes; B2, B5, B12, B13, B15, B19 , and B21 . Five types of antiserum were identified based on their reactivity to different cell subpopulations of the peripheral blood of the donor haplotype as well as in cross-reactivity for different haplotypes. RBC specific cross-reactive antigens attributed to B - G molecules were demonstrated for the B5 : B19, B12 : B19, and B19 : B21 cross-reactions. Cross-reactive antigens detected on RBC and thrombocytes attributable to B - G molecules on both types of cells were demonstrated for the B2 : B12, B2 : B15, B2 : B19, and B2 : B21 cross-reactions. In addition, cross-reactive antigens occurring on RBC and WBC were attributed to B - F (or RBC and lymphocyte-expressed B - G loci) and included the B12 : B13, B13 : B19, and B15 : B19 cross-reactions. Several antisera with specificity for B cells purportedly identifying B - L epitopes were found but their numbers were limited and cross-reactivities were not defined. The identities described here may be useful in understanding B haplotype similarities and differences in disease resistance and immune response.

Animals↗
PubMed1998

Hemagglutination pattern of galactose specific lectin from Pedilanthus tithymaloides in diabetes mellitus.

The usefulness of a galactose specific lectin from P. tithymaloides was examined to study the hemagglutination pattern in 193 patients with diabetes mellitus out of which 34 cases were of insulin dependent. A control of 72 normal subjects was also included. The hemagglutination titre against a partially purified lectin from P. tithymaloides of control group ranged from 9.1 to 170 units per mg protein with a mean value of 54 units per mg protein. Significantly low titre was observed in the cases with insulin dependent diabetes mellitus, while non-insulin dependent diabetes mellitus cases did not show any significant change. Further significant reduction in the titre in insulin dependent diabetes mellitus group was shown to occur along with the increased duration of the diabetic condition, reflecting measurable erythrocyte surface alterations.

Adolescent↗
PubMed1985

Anti-Pr cold hemagglutination associated with livedo reticularis.

A report of anti-Pr cold hemagglutination associated with livedo reticularis is presented. Livedo reticularis is descriptive of the superficial venous system appearing when blood flow is altered in this area. Cold antibody directed against the Pr antigen of the red cell membrane can cause hemagglutination, thereby altering blood flow in cooler areas of the body. This patient had livedo reticularis approximately 8 months prior to detection of the anti-Pr cold agglutinin.

Anemia, Hemolytic, Autoimmune↗
PubMed1994

Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child.

The coronavirus strain HECV-4408 was isolated from diarrhea fluid of a 6-year-old child with acute diarrhea and propagated in human rectal tumor (HRT-18) cells. Electron microscopy revealed coronavirus particles in the diarrhea fluid sample and the infected HRT-18 cell cultures. This virus possessed hemagglutinating and acetylesterase activities and caused cytopathic effects in HRT-18 cells but not in MDBK, GBK and FE cells. One of four S-specific monoclonal antibodies reacted in Western blots with HECV-4408, BCV-L9 and BCV-LY138 but not with HCV-OC43, and two reacted with BCV-L9 but not with HECV-4408, BCV-LY138 and HCV-OC43. One S-specific and two N-specific monoclonal antibodies reacted with all of these strains. cDNA encompassing the 3' 8.5 kb of the viral RNA genome was isolated by reverse transcription followed by polymerase chain reaction amplification had size and restriction endonuclease patterns similar to those of BCV-L9 and BCV-LY138. In contrast, the M gene of HCV-OC43 differed in restriction patterns from HECV-4408 and BCV. A genomic deletion located between the S and M within the non-structural genes of HCV-OC43 was not detected in HECV-4408. DNA sequence analyses of the S and HE genes revealed more than 99% nucleotide and deduced amino acid homologies between HECV-4408 and the virulent wild-type BCV. Forty-nine nucleotide and 22 amino acid differences were found between the HE genes of HECV-4408 and HCV-OC43, while only 16 nucleotide and 3 amino acid differences occurred between the HE genes of HECV-4408 and BCV-LY138. We thus conclude that the strain HECV-4408 is a hemagglutinating enteric coronavirus that is biologically, antigenically and genomically more closely related to the virulent BCV-LY138 than to HCV-OC43.

Acetylesterase↗
PubMed1993

Hemagglutination properties and nucleotide sequence analysis of the fiber gene of adenovirus genome types 11p and 11a.

The fiber has been suggested to serve as the ligand between the adenovirus capsid and the host cell receptor. The two genome types, Ad11p and Ad11a, of adenovirus serotype 11 display different tropisms. The fiber amino acid sequences of the two genome types have been deduced from the 975 nucleotides that encoded a fiber polypeptide of 35,500 Da. The fiber consists of a tail, a shaft, and a knob region. The amino acids 44 to 140 form a typical shaft domain of six 15-residue repetitive motifs. Ten amino acids in the Ad11p fiber shaft were substituted in Ad11a. Five unpolar residues have been replaced by four polar and one unpolar amino acid. In the knob region, a total of 14 amino acid mismatches were noted between Ad11p and Ad11a. The amino acid sequence Asn-Asp-Glu at positions 283 to 285 in Ad11p was changed to Arg-Ala-Asp in Ad11a. The sequence Thr-Leu-Trp-Thr from positions 133 to 136 was conserved in all analyzed human and canine adenoviruses. The polypeptide at positions 235 to 244, Phe-Met-Pro-Ser-Thr-Thr-Ala-Tyr-Pro-Phe, probably contains a subgenus epitope, since it is conserved among subgenus B adenoviruses. Ad11p aggregated rhesus and vervet erythrocytes at 37 degrees, 22 degrees, and at 4 degrees, respectively, whereas Ad11a did not display hemagglutination under the same conditions. The complete fibers of Ad11p and Ad11a share an overall amino acid homology of 92.3%. The homology within the shaft and the knob region was 89.7 and 92.4%, respectively. These variable amino acids should be expected to be responsible for the differences in hemagglutination and tropism examplified by the persistent urinary tract infections caused by Ad11p and the acute respiratory tract infections caused by Ad11a.

Adenovirus E3 Proteins↗
PubMed1994

Cloning and characterization of the cDNA encoding the HA protein of a hemagglutination-defective measles virus strain.

cDNA clones corresponding to the mRNA for the hemagglutinin of the hemagglutination-defective strain AK-1 of measles virus were isolated and characterized. Compared with the prototype Edmonston strain, 60 nucleotide substitutions that resulted in 18 amino acid changes were detected. An additional potential N-linked glycosylation site was added by point mutation, which was supported by the observation that the hemagglutinin of the AK-1 strain was stained more heavily after NaDodSO4-PAGE and periodic acid-Schiff (PAS) staining than the Edmonston strain. Computer-assisted analysis revealed that three reverse turns in the secondary structure had disappeared in the hemagglutinin of the AK-1 strain. Moreover, one of these structural changes occurred in the closely glycosylated region at amino acid residues 168-240, which appeared to be a biologically important functional domain. The isoelectric point calculated from the predicted amino acid sequence became about 1 pH unit more basic in the AK-1 strain than the Edmonston strain. This present study is the first sequence analysis of the hemagglutinin gene in a hemagglutination-defective strain of the measles virus.

Amino Acid Sequence↗
PubMed1985

Separation of plasma fibronectin from associated hemagglutinating activity by elution from gelatin-agarose at pH 5.5.

Human plasma fibronectin prepared by elution of the adsorbed protein from gelatin-agarose by pH 5.5 citrate buffer is very low in hemagglutinating activity toward trypsinized rabbit erythrocytes, an activity previously associated with the purified plasma protein. Hemagglutinating activity is present, however, in a subsequent fibronectin-poor 4M urea eluate which contains plasma immunoglobulins and/or other unidentified gelatin-binding proteins. This activity is partially inhibited by antibodies to human immunoglobulins, and the inhibition is reversed by excess non-specific human immunoglobulin.

Animals↗
PubMed1984

Identification of hemagglutinating protein and bactericidal activity in the hemolymph of adult Sarcophaga peregrina on injury of the body wall.

When the body wall of adult Sarcophaga peregrina (flesh-fly) was injured with a hypodermic needle, hemagglutinating activity and antibacterial activity were induced in the hemolymph simultaneously. The hemagglutinating activity was shown to be due to the same lectin that was found previously in the hemolymph of injured larvae. Thus, larval and adult Sarcophaga respond in the same way to injury of the body wall.

Animals↗
PubMed1977

Antigenic relationship between human coronavirus strain OC 43 and hemagglutinating encephalomyelitis virus strain 67N of swine: antibody responses in human and animal sera.

Hemagglutinating encephalomyelitis virus of swine (HEV) was adapted to growth in suckling mouse brain. Electron micrographs of HEV-infected suckling mouse brain, prepared by negative staining and thin-section techniques, exhibited typical morphological characteristics shared with other members of the Coronaviridae. The adaptation of HEV to suckling mouse brain facilitated serologic testing by the use of common host reagents and compatible animal systems. With hemagglutination inhibition, complement-fixation, and neutralization tests, an antigenic relationship was demonstrated between human coronavirus OC 43 and HEV in specific immune and hyperimmune animal sera. Children and adults with seroconversion to OC 43 antigen had diagnostic rises in titer of antibody to HEV antigens. Individuals with seroconversion to human coronaviruse 229E and B814 demonstrated antibody to HEV but not diagnostic rises in titer. Swine with titers of antibody to HEV had lower or no detectable titers of antibody to coronavirus OC 43. Although the prevalence and geometric mean titer of antibody to OC 43 were higher than the titer of antibody to HEV in every group of normal humans tested, significant differences in antibody response to coronavirus OC 43 and HEV were seen between populations that did or did not have possible contact with swine. The evidence suggested that antibody to HEV in humans probably represented a heterologous response to infection with coronavirus OC 43. However, a heterotypic response to unknown or uncharacterized strains of coronavirus cannot be excluded.

Adult↗
PubMed1977

Immune adherence hemagglutination: further observations on demonstration of antibody to varicella-zoster virus.

The immune adherence hemagglutination test for measurement of antibody to varicella-zoster (V-Z) virus is well suited to performance in a routine serology laboratory. This test is useful in assessing susceptibility to varicella, measuring antibody to V-Z virus in globulin preparations, and evaluating some effects of passive immunization. Since the complement-fixation test for antibody to V-Z virus lacks sensitivity and the fluorescent antibody to membrane antigen test is not readily available, the immune adherence hemagglutination test may be of practical value in patient management.

Antibodies, Viral↗
PubMed1984

Incorporation of sialoglycoprotein containing lacto-series oligosaccharides into chicken asialoerythrocyte membranes and restoration of receptor activity toward hemagglutinating virus of Japan (Sendai virus).

Bovine erythrocyte sialoglycoprotein (GP-2) (1) containing lactoseries oligosaccharide chains, which showed highly specific inhibition of hemagglutination by HVJ (Hemagglutinating virus of Japan, Sendai virus), was incorporated into neuraminidase-treated chicken erythrocytes which had lost their biological responsiveness to the virus. The GP-2-incorporated erythrocytes were agglutinated and lyzed again by the virus. Incorporation of 1,900 molecules of GP-2 per asialoerythrocyte restored fairly well the susceptibility of the cells to HVJ-mediated agglutination and hemolysis. Treatment of the erythrocytes with neuraminidase again resulted in the complete abolishment of the response to HVJ. The above observations are consistent with the view that exogenous sialoglycoprotein, GP-2, can be functionally integrated into the surface membrane of asialoerythrocytes and serve as the receptor for HVJ during the initial adsorption-fusion phase of the virus infection of the target cells.

Animals↗
PubMed1974

Human antibody response to three meningococcal outer membrane antigens: comparison by specific hemagglutination assays.

Three cell surface antigens, protein, lipopolysaccharide, and polysaccharide, were purified from group B and group C strains of Neisseria meningitidis representing a variety of serotypes. Chemical analysis indicated that cross-contamination was on the order of 1%. Sensitization of sheep erythrocytes with these antigens resulted in highly specific passive hemagglutination assays for the three kinds of antigens. Paired human sera from several groups of individuals were tested by hemagglutination for antibody against each of the antigens. Patients with group B or C systemic meningococcal disease showed increases in antibody titer against all three kinds of antigens, but the antibody response to B polysaccharide was low compared with the response to C polysaccharide. Nasopharyngeal carriers of group B meningococci showed significant increases in titer only against the protein antigens, and noncarriers who received a C-polysaccharide vaccine had a specific response to the C polysaccharide. A given protein or lipopolysaccharide antigen reacted on the average equally well with either group B or C convalescent sera. These results suggest that all three antigens may play a role in the broad human immunity following natural infection.

Journal Article↗
PubMed1977

Antigenic relationship between human and bovine rotaviruses as determined by neutralization, immune adherence hemagglutination, and complement fixation tests.

Guinea pig antiserum to bovine rotavirus does not neutralize human rotavirus. Bovine and human rotaviruses were, however, extensively cross-reactive when examined by complement fixation and immune adherence hemagglutination tests with antiserum to either virus. The immune adherence hemagglutination test was 16- to 32-fold more sensitive than the complement fixation test in detecting rotavirus.

Animals↗
PubMed1971

Nonspecific factors in monkey tissues and serum causing inhibition of plaque formation and hemagglutination by dengue viruses.

Normal monkey serum and the supernatant fluid from different triturated monkey tissues have been studied for the presence of nonspecific arbovirus hemagglutination and plaque forming inhibitors of dengue viruses types 1, 2, 3, and 4. Hemagglutination inhibition (HI) activity was present in most tissue specimens and demonstrated a significant gradient of effectiveness starting with, respectively, serum, spleen, adrenal, and lung having a high degree of activity, whereas skin, heart, muscle, brain, and liver demonstrated low HI titers. A slightly reversed gradient of effectiveness was obtained for the case of dengue virus inhibition of plaque formation with bile, liver, thymus, spleen, and adrenal giving high 50% plaque reduction titers and heart, muscle, serum, skin, and fat demonstrating little or no activity. Analysis by Sephadex G-200 chromatography and sucrose density gradient centrifugation suggests that HI and plaque formation inhibition are independent activities of normal serum or tissue constituents or both. Also, in addition to the physical methods of characterization, chemical treatment by absorption with kaolin or acetone extraction indicate both phenomena to be the result of the action of lipids or lipoproteins.

Journal Article↗
PubMed1984

Fractionation of hemagglutinating and bacterial binding adhesins of Bacteroides gingivalis.

An outer membrane complex containing hemagglutinating and bacterial aggregating activity has been isolated from Bacteroides gingivalis. Examination of the membrane material by biochemical analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and immunological means revealed that the crude outer membrane preparation contained three major proteins and a lipopolysaccharide population that displayed size heterogeneity. At least two membrane proteins as well as the lipopolysaccharide were found to be antigenically active by immunoblot analysis. With gel chromatography and a lipopolysaccharide disaggregating buffer the membrane material was separated into two fractions. An accompanying separation of the two adherence activities was observed. The first membrane fraction, containing mostly protein and carbohydrate material, was found to contain the bacterial aggregating activity. This fraction also contained a high-molecular-weight lipopolysaccharide population. The second membrane fraction, consisting of low-molecular-weight lipopolysaccharide, protein, and loosely bound lipid was found to contain the hemagglutinating activity.

Adhesiveness↗
PubMed1999

Requirement of MrpH for mannose-resistant Proteus-like fimbria-mediated hemagglutination by Proteus mirabilis.

Two new genes, mrpH and mrpJ, were identified downstream of mrpG in the mrp gene cluster encoding mannose-resistant Proteus-like (MR/P) fimbriae of uropathogenic Proteus mirabilis. Since the predicted MrpH has 30% amino acid sequence identity to PapG, the Galalpha(1-4)Gal-binding adhesin of Escherichia coli P fimbriae, we hypothesized that mrpH encodes the functional MR/P hemagglutinin. MR/P fimbriae, expressed in E. coli DH5alpha, conferred on bacteria both the ability to cause mannose-resistant hemagglutination and the ability to aggregate to form pellicles on the broth surface. Both a DeltamrpH mutant expressed in E. coli DH5alpha and an isogenic mrpH::aphA mutant of P. mirabilis were unable to produce normal MR/P fimbriae efficiently, suggesting that MrpH was involved in fimbrial assembly. Amino acid residue substitution of the N-terminal cysteine residues (C66S and C128S) of MrpH abolished the receptor-binding activity (hemagglutinating ability) of MrpH but allowed normal fimbrial assembly, supporting the notion that MrpH was the functional MR/P hemagglutinin. Immunogold electron microscopy of P. mirabilis HI4320 revealed that MrpH was located at the tip of MR/P fimbriae, also consistent with its role in receptor binding. The isogenic mrpH::aphA mutant of HI4320 was less able to colonize the urine, bladder, and kidneys in a mouse model of ascending urinary tract infection (P < 0.01), and therefore MR/P fimbriae contribute significantly to bacterial colonization in mice. While there are similarities between P. mirabilis MR/P and E. coli P fimbriae, there are more notable differences: (i) synthesis of the MrpH adhesin is required to initiate fimbrial assembly, (ii) MR/P fimbriae confer an aggregation phenotype, (iii) site-directed mutation of specific residues can abolish receptor binding but allows fimbrial assembly, and (iv) mutation of the adhesin gene abolishes virulence in a mouse model of ascending urinary tract infection.

Adhesins, Bacterial↗
PubMed1965

Mode of Action of an Inhibitor from Agar on Growth and Hemagglutination of Group A Arboviruses.

Colón, Julio I. (Fort Detrick, Frederick, Md.), Jane B. Idoine, Orville M. Brand, and Richard D. Costlow. Mode of action of an inhibitor from agar on growth and hemagglutination of group A arboviruses. J. Bacteriol. 90:172-179. 1965.-A polysaccharide obtained from agar, and having properties similar to a previously described sulfated polysaccharide, was observed to inhibit growth and hemagglutination of some group A arboviruses. The evidence presented confirms that the inhibitory activity, in part, is the result of direct interaction between the agar polysaccharide (AP) and free virus particles. Additional evidence indicates that inhibition of viral growth also occurs as the result of interaction between AP and the chick-fibroblast cells used for propagation of the virus. The possibility was considered, therefore, that at least two different inhibitors could be present in AP-one that reacts directly with the virus particle and another that reacts with host cells. AP does not induce the production of interferon in the test system used.

Journal Article↗
PubMed1982

Revertant analysis of a temperature-sensitive mutant of Newcastle disease virus with defective glycoproteins: implication of the fusion glycoprotein in cell killing and isolation of a neuraminidase-deficient hemagglutinating virus.

Biological and molecular properties of a temperature-sensitive mutant (C1) of Newcastle disease virus and its revertants were analyzed. C1 exhibited three temperature-sensitive alterations (plaque formation, virion assembly, and cytopathogenicity) and several defects which were also present at the permissive temperature. C1 virions contained low amounts of hemagglutinin-neuraminidase glycopeptides and consequently were deficient in hemagglutinating and neuraminidase activities. These virions also contained defective fusion glycoproteins which rendered them poorly hemolytic and slow to penetrate cultured chicken embryo cells. The biological activities of the membrane glycoproteins were recovered sequentially in a series of plaque-forming revertants. The coreversion of hemolysis, membrane-penetrating activities, and cytopathogenicity in the first-step revertant (S1) suggested that fusion glycoproteins were major contributors to cellular destruction. This revertant also provided evidence of a role for fusion glycoproteins in virion assembly. From S1 we isolated a large-plaque-forming revertant (L1) that assembled wild-type amounts of biologically active hemagglutinin-neuraminidase glycoproteins into virions. Although it was normal for hemagglutination, L1 had less than 3% of the neuraminidase activity of the wild type, demonstrating that these two activities can be uncoupled genetically. The neuraminidase deficiency of L1 did not impair its virulence in ovo or its reproduction in cultured cells.

Animals↗