Streptococcal M protein: molecular design and biological behavior

Fischetti, Vincent A.

doi:10.1128/cmr.2.3.285

Cited by 761 publications

(495 citation statements)

References 209 publications

Supporting

Mentioning

482

Contrasting

Unclassified

Order By: Relevance

“…Among such proteins, particular attention has been given to the scarlet fever toxins as well as to the M proteins, the antiphagocytic fibrils extending from the bacterial cell surface [4]. In addition to these well-studied proteins, some strains of group A streptococci are also known to express a cell-surface receptor with affinity for the Fc part of IgA or IgG [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Binding of IgA and/or IgG is a common property among clinical isolates of group A streptococci

Lindahl

Stenberg

1990

Epidemiol. Infect.

View full text Add to dashboard Cite

SUMMARYCertain strains of group A streptococci are known to bind IgA and/or IgG via a cell surface receptor, which may act as a virulence factor. The distribution of such receptors among routine clinical isolates was studied, using a total of 225 strains and an assay based on the binding of radiolabelled immunoglobulins. Among 194 throat strains isolated during three different time periods in two different geographical areas of Sweden, 82% showed significant binding of IgA and/or IgG. Studies on 31 septicaemia strains, isolated over a period of more than 8 years, showed binding for 84% of the isolates. The binding strains were of several different T-types and could be subdivided into two groups, those binding both IgA and IgG and those binding IgG only. These data show that binding of IgA and/or IgG is a very common property among clinical isolates of group A streptococci.

show abstract

Section: Introductionmentioning

confidence: 99%

Binding of IgA and/or IgG is a common property among clinical isolates of group A streptococci

Lindahl

Stenberg

1990

Epidemiol. Infect.

View full text Add to dashboard Cite

show abstract

“…The M protein inhibits phagocytosis by human neutrophils and allows S. pyogenes to grow rapidly in whole human blood [3]. In addition, M protein may have other functions, such as promoting adhesion to human epithelial cells [4].…”

Section: Protein and Its Role In Phagocytosis Resistancementioning

confidence: 99%

“…Several lines of evidence indicate that M protein plays a major role in human infections [3]. For example, recent studies in a primate model of S. pyogenes infection demonstrated that M protein promotes pharyngeal colonization, a feature that may be explained by its antiphagocytic property and/or by its ability to promote adhesion to epithelial cells [5].…”

Section: Protein and Its Role In Phagocytosis Resistancementioning

confidence: 99%

“…The M protein is stable within a single strain, but exhibits extensive sequence variability between strains, in particular in the Nterminal so-called hypervariable region (HVR), which determines the M type of the strain. Antibodies directed against the HVR are protective and the immunity is type-specific [3,7]. In other words, M protein exhibits antigenic variation.…”

Section: Protein and Its Role In Phagocytosis Resistancementioning

confidence: 99%

“…A priori, the M protein would appear to be a promising vaccine component, because it is expressed by all strains and elicits protective immunity, but the antigenic variation between M proteins expressed by different strains has so far precluded the development of a vaccine. Moreover, possible cross-reactions between M protein and human tissues have caused major concerns [3]. However, work is in progress to develop a multivalent vaccine based on a combination of many different HVRs, which may not elicit unwanted cross-reactivities [33].…”

Section: Vaccine Development: a Problem With Animal Modelsmentioning

confidence: 99%

See 2 more Smart Citations

Host–pathogen interactions in Streptococcus pyogenes infections, with special reference to puerperal fever and a comment on vaccine development

Areschoug

Carlsson

Stålhammar‐Carlemalm

et al. 2004

Vaccine

View full text Add to dashboard Cite

Host-pathogen interactions in Streptococcus pyogenes infections, with special reference to puerperal fever and a comment on vaccine development. Link to publication Citation for published version (APA): Areschoug, T., Carlsson, F., Stålhammar-Carlemalm, M., & Lindahl, G. (2004). Host-pathogen interactions in Streptococcus pyogenes infections, with special reference to puerperal fever and a comment on vaccine development. Vaccine, 22 Suppl 1(Suppl 1), S9-S14. DOI: 10.1016DOI: 10. /j.vaccine.2004 General rights Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights.• Users may download and print one copy of any publication from the public portal for the purpose of private study or research.• You may not further distribute the material or use it for any profit-making activity or commercial gain • You may freely distribute the URL identifying the publication in the public portal

show abstract

Assessment of the interaction of human complement regulatory proteins with group AStreptococcus. Identification of a high-affinity group AStreptococcus binding site in FHL-1

et al. 2000

View full text Add to dashboard Cite

Group A Streptococcus (GAS), the most frequent bacterial cause of suppurative infections in humans, expresses on the cell surface M proteins with capacity to bind factor H, FHL‐1 and C4b binding protein (C4BP). This has been interpreted as a mechanism developed by this pathogen to decrease phagocytosis by macrophages and polymorphonuclear cells. We report the analysis of the capacity to bind factor H, FHL‐1 and C4BP of 69 clinical isolates from 19 different serotypes. We show that strains binding complement regulators (30 / 69) belong to specific M serotypes. Of these, M18 strains are relatively frequent and interact with all three complement regulators simultaneously. However, the most virulent M1 and M3 strains did not bind complement regulators in our assays. The relevance of the interaction between complement regulators and S. pyogenes was analyzed using different approaches with the conclusion that under physiological conditions only FHL‐1 and C4BP bind to streptococci. We show that FHL‐1 presents a higher binding affinity for S. pyogenes than factor H because it carries a hydrophobic, high‐affinity, GAS binding site in addition to the heparin binding site in SCR7. Using synthetic peptides we provide evidence that the high‐affinity GAS binding site in FHL‐1 involves the hydrophobic tail (Ser‐Phe‐Thr‐Leu) that distinguishes FHL‐1 from factor H.

show abstract

Streptococcal M protein: molecular design and biological behavior

Cited by 761 publications

References 209 publications

Binding of IgA and/or IgG is a common property among clinical isolates of group A streptococci

Binding of IgA and/or IgG is a common property among clinical isolates of group A streptococci

Host–pathogen interactions in Streptococcus pyogenes infections, with special reference to puerperal fever and a comment on vaccine development

Assessment of the interaction of human complement regulatory proteins with group AStreptococcus. Identification of a high-affinity group AStreptococcus binding site in FHL-1

Contact Info

Product

Resources

About