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Biomedical subjects

G H Stollerman

Publications and source records attributed to G H Stollerman.

At least 19 recordsLinked to original sources
PubMed1991

Rheumatogenic streptococci and autoimmunity.

The uniqueness of the group A streptococcus in initiating a cardiodestructive disease in a limited segment of the human species, regardless of race or ethnic group, makes the quest for a unique host response to a specific streptococcal antigen an intriguing and persisting challenge for clinical investigators, particularly for those investigators interested in autoimmunity. New methodology is making possible more incisive research approaches. The defined streptococcal antigens that turn out to be epitopes identical with host tissues, such as the M protein/cardiac myosin model or the hyaluronate in the capsule of mucoid rheumatogenic strains, offer the opportunity for more incisive clinical investigations. The isolation and cultivation of cardiotoxic T cell clones directed against such epitopes shared by host and parasite may eventually be possible. We may then learn more about whether autoimmunity is indeed a factor in the pathogenesis of rheumatic heart disease.

Acute Disease↗
PubMed1989

Valedictory.

Explore the source record for details and available documents.

Geriatrics↗
PubMed1979

Human immune response to immunization with a structurally defined polypeptide fragment of streptococcal M protein.

We tested the ability of pepsin-extracted, highly purified M protein to induce type-specific immunity in experimental animals and humans. M protein was prepared from limited peptic digests of whole group A type 24 streptococci and was purified to chemical homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, quantitative amino acid analysis, and Edman degradation. For vaccination, the lyophilized M24 protein preparation (pep M24) was precipitated in aluminum hydroxide. When injected into laboratory animals, alum-precipitated pep M24 produced type-specific protective antibodies and was free of non-type-specific immunoreactivity. In man, skin tests with 1-microgram doses of pep M24 were negative in all 37 adults tested. 12 adult human volunteers received two-four subcutaneous injections of 100-200 micrograms of alum-precipitated pep M24 at intervals of at least 2 wk. The immune response to pep M24 was measured by a variety of assays designed to detect (a) type-specific humoral antibodies (opsonophagocytic, long chain, and mouse protection tests); (b) total humoral antibodies (complement fixation and enzyme-linked immunosorbent assay); (c) cellular immunity (skin tests); and (d) heart cross-reactive antibodies (immunofluorescence). Type-specific opsonic antibodies developed in 10 of the 12 vaccinees, and positive delayed-type skin tests developed in 11. Immune sera from two of the vaccinees were effective in mouse-protection tests against challenge with M24 but not M6 streptococci. None of the volunteers developed heart-reactive antibodies or antibodies to non-type-specific M protein antigens. Alum-precipitated pep M24 was well-tolerated in man, and no serious local or systemic reactions were observed. Thus, pep M24 induces type-specific, protective antibodies in doses that are well-tolerated in man.

Adult↗
PubMed1978

Trends in bacterial virulence and antibiotic susceptibility: streptococci, pneumococci, and gonococci.

Antibiotic usage and improved living conditions may have contributed to a dilution of "rheumatogenic" strains of group A streptococci and to their replacement by attenuated streptococci with less rheumatogenic potential. Whether this is due to decreased virulence or to loss of specific bacterial antigens or toxins in prevalent strains is not yet known. The pneumococcus, which has been moderately resistant to antibiotics only in isolated cases, has appeared in South Africa in strains that are highly resistant to at least five major antibiotics; plasmid transmission of resistance is suspected. The newly available pneumococcal vaccine may become very important if such strains spread. Gonococci isolated from urogenital lesions have developed only moderate drug resistance. Gonococci causing disseminated infection have retained their exquisite sensitivity to penicillin; the most virulent strains are associated with greatest sensitivity. However, the newly discovered penicillinase-plasmid in gonococci is transferable to these virulent strains as readily as to others.

Anti-Bacterial Agents↗
PubMed1977

Purification and properties of M protein extracted from group A streptococci with pepsin: covalent structure of the amino terminal region of type 24 M antigen.

M protein was extracted from type 24, group A streptococci with pepsin at pH 5.8 and was further purified by ammonium sulfate precipitation, ribonuclease digestion, ion-exchange chromatography, and isoelectric focusing. The purified pepsin extract of M (pep M) protein was shown to be free of nontype-specific immunoreactivity in (a) complement fixation tests with heterologous M antiserum, (b) skin tests in normal adult guinea pigs, and (c) passive hemagglutination tests for the presence of lipoteichoic acid sensitizing or antigenic activity. The pep M24 was highly immunogenic; two of three rabbits developed opsonic antibody titers of 1:256 and the third a titer of 1:32 6 wk after a single injection of 100-pg doses of pep M24 emulsified in complete Freund's adjuvant. The antisera lacked nontype-specific antibodies and produced single precipitin lines in agar gel diffusion tests against crude HC1 extracts of the homologous M protein. Thus, the type-specific antigenic determinant(s) of type 24 M protein appears to be separable from immunotoxic, cross-reactive antigens without loss of immunogenicity in rabbits. The mobility of pep M24 upon electrophoresis in 10 percent sodium dodecyl sulfate pelyacrylamide gel was consistent with an average mol wt of 33,500 daltons. Amino acid analysis demonstrated a predominance of alanine, followed by glutamic acid, lysine, leucine, and aspartic acid. Pep M24 contained an estimated six to seven methionine residues and approximately ten phenylalanine residues per molecule. No other aromatic amino acids were detected. Automatic Edman degradation of pep M24 yielded the sequence of the first 29 amino acids (the amino terminal amino acid being valine) of the amino terminal region of the molecule. The detection of only one new amino acid at each step of Edman degradation confirmed the homogeneity of the purified pep M24.

Amino Acid Sequence↗
PubMed1977

Streptococcal infections that fail to cause recurrences of rheumatic fever.

Prospective studies of recurrences of streptoccal infection and acute rheumatic fever were conducted among patients attending the acute rheumatic fever prophylaxis clinic (City of Memphis Hospitals, Memphis, Tennessee) between 1965 and 1972. The patient population consisted of 124 rheumatic children and adults, two-thirds of whom had evidence of rheumatic heart disease. A total of 104 immunologically documented streptococcal infections occurred during 235 patient-years of follow-up (44.3 infections per 100 patient-years) without a single recurrence of rheumatic fever. Immune responses tended to be modest, and 80% of the infections were subclinical. The majority of our group A streptococcal isolates were obtained from routine cultures of specimens from asymptomatic individuals. Many of these strains were "pyoderma" serotypes, whereas others exhibited a characteristic (production of opacity factor) recently reported to be associated with decreased immunogenicity. Several factors may have contributed to the low recurrence rate of acute rheumatic fever, including the age range of the population under study and immunologically significant infections with strains of Streptococcus that were not group A, but a major reason may be the possibility that the group A strains prevalent in this population have diminished rheumatogenic potential.

Adolescent↗