M proteins are the major pathogenicity factors of Streptococcus pyogenes

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Abstract

M proteins are the major pathogenicity factors of the widespread and potentially deadly bacterial pathogen Streptococcus pyogenes. These proteins confer to bacteria resistance against innate and adaptive immune responses. The study of the M proteins of hemolytic streptococci group A and their involvement in pathology clearly indicates that strains of streptococci, for one reason or another devoid of M proteins are unable to multiply in the macroorganism and form a focus of infection. This circumstance in itself once again underlines the leading role of M proteins in the realization of its many properties and in the development of the infectious process. The ability of M proteins to recruit plasma proteins of the macroorganism is their significant pathogenetic properties. The most important is the nonimmune binding by M proteins of human immunoglobulins, because it participates in the suppression of phagocytosis, violations of bacterial opsonization and complement activation along the classical pathway, not to mention the possible involvement of this phenomenon in the genesis of post-infectious complications of autoimmune nature. This review summarizes the current data on the structure M proteins, their functional activity, manifestations of pathogenicity, genetic regulation and methods of emm-typing.

About the authors

Larisa A. Burova

Institute of Experimental Medicine

Author for correspondence.
Email: lburova@yandex.ru
ORCID iD: 0000-0001-7687-2348
SPIN-code: 6084-1255
Scopus Author ID: 7003982261
ResearcherId: E-5270-2014

MD, Dr. Sci. (Med.), Leading Research Associate, Department of Molecular Microbiology

Russian Federation, Saint Petersburg

Alexander N. Suvorov

Institute of Experimental Medicine

Email: alexander_suvorov1@hotmail.com
ORCID iD: 0000-0003-2312-5589
SPIN-code: 8062-5281
Scopus Author ID: 7101829979
ResearcherId: J-6921-2013

MD, Dr. Sci. (Med.), Professor, Corresponding Member of the Russian Academy of Sciences, Head Department of Molecular Microbiology

Russian Federation, Saint Petersburg

Artem A. Totolian

Institute of Experimental Medicine

Email: totolyan@hotmail.com
ORCID iD: 0000-0002-3310-9294
SPIN-code: 1741-9171
Scopus Author ID: 57194530404
ResearcherId: J-4218-214

MD, Dr. Sci. (Med.), Professor, Academician RAS, Chief Research Associate, Department of Molecular Microbiology

Russian Federation, Saint Petersburg

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2. Fig. 1. Typical appearance of Streptococcus pyogenes on the surface of 5% blood agar 18-hours incubation under aerobic conditions

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3. Fig. 2. Characterization of the complete sequence of Streptococcus pyogenes M6 protein [1]. The M6 protein of S. pyogenes consists of four domains: A, B, C and D; N — terminal fragment of the M protein; C is the region of attachment of the M protein to the cell wall of the microbe; LPXTG — anchor sequence pattern

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4. Fig. 3. Genetic organization of the Mga-regulon of Streptococcus pyogenes [35]: Mga is a regulator of a number of GAS genes, the most notable of which are the family of M proteins whose genes are tandem linked: emm encodes a type-specific Eмм protein, mrp and enn encode M-like proteins, scpa encodes peptidase C5a. Some serotypes contain only mga, emm and scpa (pattern A). Other serotypes contain one or more remaining genes (patterns B–E)

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5. Fig. 4. The ability of M and M-like proteins Streptococcus pyogenes to bind human plasma proteins [32]. On the left is a diagram of the M protein molecule covalently attached to the streptococcal cell wall; on the right — M and M-like proteins on the surface of the streptococcal cell wall. M and M-like proteins bind non-immune human IgG and IgA, C4BP, factor H (FH), fibrinogen (Fg), plasminogen (Pla); they are also able to block the deposition of opsonins such as C3b and type-specific antibodies

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