Repetitive sequences in protein a from <i>Staphyloccus aureus</i>: Three highly homologous Fc‐binding regions

Sjödahl, Jörgen

doi:10.1016/0014-5793(76)80871-x

Cited by 25 publications

(10 citation statements)

References 27 publications

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“…However, cell-bound protein A from the parental strain had no free N-terminal amino acid as previously reported (25). As described earlier by Sjodahl (21,22) protein A is built up by four structurally similar regions, each of which is able to react with IgG. The four regions, all having a molecular weight of 7,000, are located close together in the N-terminal part of the protein A molecule.…”

Section: Discussionsupporting

confidence: 69%

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Physico‐ and Immunochemical Properties of Staphylococcal Protein A Extracellularly Produced by a Set of Mutants from Staphylococcus aureus Cowan I

Movitz

Masuda

Sjöquist

1979

Microbiology and Immunology

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Section: Discussionsupporting

confidence: 69%

“…The molecule has four sites to which IgG can bind, each of which is located in a structure with a molecular weight of 7,000. The amino acid sequences of these four structures reveal a high homology (21)(22)(23).…”

mentioning

confidence: 97%

Physico‐ and Immunochemical Properties of Staphylococcal Protein A Extracellularly Produced by a Set of Mutants from Staphylococcus aureus Cowan I

Movitz

Masuda

Sjöquist

1979

Microbiology and Immunology

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“…Staphylococcal protein A is another bacterial surface protein that resembles M protein in antiphagocytic activity (32), amino acid composition (33), extended shape (34), and internally repetitive sequences (33,35). Protein A is composed of four highly homologous regions, each consisting of 58 amino acid residues, which are capable of binding the Fc region of IgG (35).…”

mentioning

confidence: 99%

Amino acid sequence and physicochemical similarities between streptococcal M protein and mammalian tropomyosin.

Hosein¹,

McCarty²,

Fischetti³

1979

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACr-The amino-terminal sequences of two peptides of type 24 streptococcal M protein show similarities with that of rabbit skeletal muscle tropomyosin, having up to 40% identical residues and probabilities of occurring by chance as low as P < 10-5. In addition, a hexapeptide (Glu-Ala-Glu-Lys-AlaAla) that is found five times in the M24 protein was shown to be identical to a sequence in tropomyosin. Similarities are also seen in the amino acid compositions and physicochemical properties of tfie two proteins. The amino-terminal sequences of peptides from another bacterial surface protein, staphylococcal protein A, are highly correlated with segments of two other myofibrillar proteins, rabbit actin (P < 10-7) and rabbit myosin Al light chain (P < 10-6). The data presented suggest that a close structural relationship exists between mammalian muscle proteins and the biologically active surface proteins of staphylococci and streptococci. In addition, the correlation between sequences in M protein and tropomyosin represents direct evidence of a structural similarity at a molecular level between a streptococcal protein and a mammalian muscle component and may therefore prove relevant to the pathogenicity of the streptococcus.Group A streptococci possess antiphagocytic surface antigens, known as M proteins, that are primarily responsible for the virulence of these organisms (1). Based on extensive immunological data, it has been clearly shown that resistance to streptococcal infection is dependent on neutralization of the antiphagocytic effect of M proteins by type-specific opsonic antibodies (1, 2). Immunological cross reactions do occur' between certain of the more than 70 immunologically distinct M types (3, 4), but the antibodies involved rarely afford crossprotection (3). Recent peptide analyses (5) and sequence studies (6, 7) on a limited number of M protein types revealed that, in spite of a common biological activity, M proteins are composed of different primary structures. Despite these immunological and structural differences, all M protein molecules studied to date share certain noteworthy chemical and physical properties (8). Their extreme thermal stability (9), their highly elongated shape (10, 11), and their appearance as a network of projections on streptococcal cell walls (12) suggested that M proteins might have properties in common with previously characterized fibrous proteins.This report describes striking chemical, physical, and sequence similarities between streptococcal M protein and rabbit skeletal muscle tropomyosin. In addition, computer analysis of the partial sequence of staphylococcal protein A, another biologically active, Gram-positive, surface protein, having properties in common with M protein, reveals significant homology with two other myofibrillar proteins, actin and myosin Al light chain.

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“…Preliminary experiments showed that the addition of protein A to large soluble preformed antigen-antibody complexes rendered these aggregates insoluble. To circumvent this problem, active, monovalent tryptic fragments of protein A were prepared [14,15] and used in titration experiments of soluble antigen-antibody complexes. Three different monoelonal antibodies (45-394, GE-10(A) and GE-IO(C)) and one antibody of restricted heterogeneity (30-267) to two noncrossreactive pneumococcal polysaccharide antigens (SII and Sill) were used and their reaction with oligosaccharide haptens could be also followed by quenching or enhancement of antibody fluorescence.…”

Section: Resultsmentioning

confidence: 99%

Independence of the binding of domain‐specific ligands to Fab and Fc suggests that antigen‐induced effects in IgG antibodies are not allosteric

Wright¹,

Engel²

1978

FEBS Letters

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Repetitive sequences in protein a from Staphyloccus aureus: Three highly homologous Fc‐binding regions

Cited by 25 publications

References 27 publications

Physico‐ and Immunochemical Properties of Staphylococcal Protein A Extracellularly Produced by a Set of Mutants from Staphylococcus aureus Cowan I

Physico‐ and Immunochemical Properties of Staphylococcal Protein A Extracellularly Produced by a Set of Mutants from Staphylococcus aureus Cowan I

Amino acid sequence and physicochemical similarities between streptococcal M protein and mammalian tropomyosin.

Independence of the binding of domain‐specific ligands to Fab and Fc suggests that antigen‐induced effects in IgG antibodies are not allosteric

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