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Biomedical subjects

G R Dreesman

Publications and source records attributed to G R Dreesman.

At least 19 recordsLinked to original sources
PubMed1979

Detection of herpesvirus type-specific antibody by a micro solid phase radioimmunometric assay.

A micro solid phase radioimmunometric assay has been developed which measures type-specific antibody in human sera to herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2). The test is performed by coating wells of microtiter plates with purified HSV-specified glycoproteins, VP123 and VP119, derived from HSV-1- and HSV-2-infected cells, respectively. The coated wells are then incubated with diluted unadsorbed sera and subsequently with radioiodinated goat anti-human IgG reagent. Because these major viral envelope glycoproteins contain type-specific antigenic determinants, type-specific antibodies are preferentially detected in our assay.

Antibodies, Viral↗
PubMed1978

Cellular and humoral immunity in guinea pigs to two major polypeptides derived from hepatitis B surface antigen.

Guinea pigs immunized with hepatitis B surface antigen (HBsAg), types adw, adr and ayw, and with two major polypeptides derived from HBsAg/adw developed cell-mediated immunity as determined by the macrophage migration inhibition assay. Peritoneal exudate cells from animals immunized with a 22000- or a 25000-mol. wt. polypeptide derived from HBsAg/adw showed significant migration inhibition after challenge with either polypeptide or with purified HBsAg. Significant inhibition of macrophage migration was not observed when polypeptide-sensitized cells were challenged with normal human serum or with normal human liver extract. Similarly, a cell-mediated immune response was not observed in peritoneal exudate cells from animals sensitized to normal human serum or normal human liver extract which were challenged with either of the polypeptides. The humoral immune response to either of the polypeptides, as measured by radioimmunoassay, was substantially lower than that observed in animals immunized with intact particles. This apparent difference between cellular and humoral responses suggests that the macrophage migration assay is a sensitive indicator of the immunogenicity of the smaller mol. wt. HBsAg-derived polypeptides in guinea pigs.

Animals↗
PubMed1978

Immunoglobulin-specific radioimmunoprecipitation assays for quantitation of nasal secretory antibodies to hemagglutinin of type A influenza viruses.

Radioimmunoprecipitation (RIP) assays were developed to selectively quantitate class-specific antibodies to purified hemagglutinins (HA) of type A influenza virus in nasal secretions. Rabbit anti-human secretory piece of immunoglobulin A (IgA) and rabbit anti-human IgG were used as second antibodies. A third antibody, goat anti-rabbit IgG, was incorporated into the system to separate immune complexes formed between iodinated HA, nasal wash test specimen, and second antibody. The utilization of this reagent avoided the need for large quantities of IgA and IgG antibody-negative carrier secretions. Nasal was specimens obtained from 14 adults immunized with an inactivated type A influenza virus vaccine were evaluated by RIP and viral neutralization assays. Significant homologous postvaccination secretory IgA and IgG antibody levels were demonstrable in 13 (93%) of individuals by RIP, whereas only 5 (36%) exhibited rises by viral neutralization tests. Moreover, the geometric mean IgA and IgG antibody levels were at least 20- and 37-fold greater than the neutralizing antibody titer. The pattern of heterologous immunoglobulin-specific antibody responses tended to be similar to those observed with the homologous HA subunit.

Adult↗
PubMed1978

Coxsackievirus aggregates in muscle cells of a polymyositis patient.

Muscle biopsy specimens of a patient with polymyositis showed crystalline structures resembling picornavirus aggregates within muscle cells. The patient's serum reacted in an indirect immunofluorescence assay with autologous muscle cells. A strongly positive immunofluorescence staining was also noted when a section of muscle tissue was reacted with coxsackievirus A9 antiserum, and a weakly positive reaction was noted with coxsackievirus B2 antiserum. No staining was observed after treatment with antiserum to poliovirus type 1 or echovirus types 11 and 22.

Aged↗
PubMed1977

Viral hepatitis.

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Hepatitis B Antigens↗
PubMed1977

Biochemical and biophysical properties of hepatitis B core particles derived from Dane particles and infected hepatocytes.

Hepatitis B core antigen (HBcAg) was purified from Dane particles and from infected hepatocytes. An identical isoelectric pH of 4.0 was determined for labeled preparations of both Dane-derived and liver-derived HBcAg. Unlabeled liver-derived HBcAg demonstrated a lower isoelectric pH of 3.7. Molecular weight determinations by Sepharose 4B column chromatogrpahy revealed that liver-derived HBcAg had a molecular weight of 8.5-9.0 X 10(6) daltons. The sedimentation coeficient of both Dane- and liver-derived HBcAg was found to be 124S. PAGE revealed that iodinated HBcAg derived from Dane particles was very similar in polypeptide structure to HBcAg derived from infected liver tissue. Twelve polypeptides were resolved from Dane core particles, and seven to nine were resolved from liver core particles. Several of the polypeptides in both preparations co-migrated with iodinated hepatitis B surface antigen (HBsAg). However, three polypeptides (mol. wt. 88,000, 79,000 and 59,000) were found in both Dane- and liver-derived HBcAg but not in HBsAg, which suggests that these polypeptides are HBcAg-specific. Endogenous DNA polymerase activity was observed in both Dane- and liver-derived core particles.

DNA-Directed DNA Polymerase↗
PubMed1976

Studies on herpes simplex virus and cancer.

Virus-induced polypeptides of cells infected by herpes simplex virus (HSV) types 1 and 2 were investigated by analysis on polyacrylamide gels and by determination of their antigenicity. Some polypeptides, VP154 and VP134, had immunological reactivity common to both virus types, while others (VP175 and VP123) were type specific. Only the glycosylated polypeptides were able to induce neutralizing antibody. The expression of viral genetic information was studied in newborn mice infected with wild-type and ts mutant viruses; some mutants had become attenuated and had lost pathogenicity for newborn mice while others had not. From induction experiments in HSV=transformed hamster cells, it appears that detection of enhanced replication of ts mutants in human cancer cells would be an indication of resident HSV genetic information. Sera obtained from cancer patients were examined for antibodies to early proteins synthesized in HSV-infected cells. The method used was an indirect radioimmune precipitation test followed by polyacrylamide gel electrophoretic analysis of immune precipitates. Cervical cancer patients had sera with a higher reactivity to early nonstructural polypeptides than to breast cancer patients or to matched healthy women. In contrast to the results with early polypeptides, little difference was detectable between the matched sera in their reactivity with a major capsid polypeptide, which is synthesized late in the infectious cycle.

Animals↗
PubMed1976

Detection of viral hepatitis type A.

Several technics are currently being used to detect hepatitis type A antigen or its antibody. These include immunoelectronmicroscopy, immune adherence, and complement fixation. This paper describes another promising technic, a microtiter solid-phase immunoradiometric assay, in which hepatitis A antigen and antibody are detected. Such a method can be utilized for biochemical and biophysical analysis of purified particles, for the seroepidemiology of type A hepatitis, and as a means for monitoring hepatitis A antigen in cell cultures.

Animals↗
PubMed1975

Immunological and biophysical properties of hepatitis B antigen labeled by the chloramine-T and by the lactoperoxidase methods.

Optimal conditions were sought for the radiolabeling of microgram quantities of hepatitis B surface antigen (HBs Ag) employing the chloramine-T or lactoperoxidase iodination procedures. Preparations of HBsAg labeled by these procedures are referred to as chloramine-T preparations and lactoperoxidase preparations, respectively. Labeled HBsAg having specific activities between 10-20 muCi/mug were found to display the greatest degree of sensitivity for unlabeled HBsAg and for anti-HBs using a double-antibody radioimmunoassay (RIA-DA). Increasing the specific activity above this level redulted in a decreased affinity of labeled 1251-HBs Ag for anti-HBs, indicating that soluble antigenic alterations had developed. At equivalent specific activities, chloramine-T preparations competed less effectively for unlabeled HBs Ag than lactoperoxidase preparations, and anti-HBs endpoint titers were slightly reduced, especially among preparations of high specific activity (greater than or equal to 65 muCi/mug). Chloramine-T preparations of HBs Ag (sp. act. 15--30 muCi/mug) showed essentially no antigenic deterioration over a 2-month period at minus 196 degrees C or minus 70 degrees C. Utilization of optimally labeled 1251-HBs Ag has increased the sensitivity of the RIA-DA for unlabeled HBs Ag 30-fold to a level below 1 ng/ml and enhanced antiamine-T method revealed that only the most acidic population was labeled (pH 3.75+/-0.5). In contrast, six antigenic components with distinct pI values ranging from 3.7 to 5.2 were detected by RIA-DA in both unlabeled HBs ag and in the chloramine-T preparation. This indicated that the chloramine-T method did not radically change the relative number or charge of each of the pI populations present in purified preparations of HBs Ag. Analysis of HBs Ag iodinated by the lactoperoxidase procedure revealed the presence of three of four populations of particles with pI values ranging from 3.9 to 4.5, suggesting that this procedure labels HBs Ag more uniformly.

Chloramines↗
PubMed1975

Cell-mediated immunity in guinea pigs to subunits derived from hepatitis B surface antigen.

Guinea pigs immunized wit- hepatitis B surface antigen (HBSAg), types adw and ayw, and with two polypeptides (400,000 and 24,000 molecular weight) developed cell-mediated immunity (CMI), as determined by radioimmunoassay. Peritoneal exudate (PE) cells from guinea pigs immunized with the 40,000-molecular-weight polypeptide migrated poorly (30 to 88% inhibition) after challenge with the immunizing subunit or with purified HBSAg, type gdw or ayw. Response of the same PE cells to the 24,000-molecular-weight subunit was significantly reduced. Similar but less striking evidence for CMI was observed was PE cells derived from guinea pigs inoculated with purified type-specific HBSAg or with the 24,000-molecular-weight polypeptide. Humoral responses were predictable and showed a reasonable degree of correlation with the CMI response. PE cells from control animals inoculated with normal human serum or polyacrylamide gel were not inhibited after challenge with purified preparations of HBSAg or with the 400,000-molecular-weight polypeptide, but did show CMI with their respective immunogens. In addition, PE cells from guinea pigs inoculated with normal human serum were inhibited from migrating after challenge with the 24,000-molecular-weight subunit, suggesting that the latter may contain an antigenic determinant related to a human serum protein.

Animals↗
PubMed1975

Comparative biophysical studies of hepatitis B antigen, subtypes adw and ayw.

Comparative biophysical and biochemical analyses were performed on purified preparations of hepatitis B antigen (HBs Ag) subtypes adw and ayw, including isoelectric pH evaluations, analysis of the different morphological forms, molecular weight determinations, and analysis of the polypeptides by polyacrylamide gel electrophoresis, Both HBs Ag-positive plasma and purified HBs Ag were analyzed by electrofocusing in a sucrose ampholyte gradient. Four distinct populations of HBs Ag with a pH range of 4.5 plus or minus 0.1 to 5.4 plus or minus 0.1 for unfractionated plasma samples and 3.9 plus or minus 0.05 to 4.9 plus or minus 0.05 for purified samples were detected in both adw and ayw preparations. Electron microscopic studies of each population of purified HBs Ag revealed 19- to 27-nm spheres in each fraction. Purified material labeled with 125I by the chloramine-T method behaved as one major population with an isoelectric pH value of 3.9 plus or minus 0.1. Purified adw preparations revealed a major population with a molecular weight of 3.7 times 10-6 and a second one of 4.6 times 10-6. Purified preparations of ayw contained one population with a molecular weight of 4.6 times 10-6. Polyacrylamide gel electrophoretic analysis of purified HBs Ag revealed nine polypeptides for ayw and seven for adw particles. These studies indicate that purified preparations of HBs Ag are heterogeneous and that distinct differences can be detected between the two subtypes.

Centrifugation, Density Gradient↗