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Identification and characterization of a second extracellular collagen-like protein made by group A Streptococcus: control of production at the level of translation.

ABSTRACT: A recent study found that group A Streptococcus (GAS) expresses a cell surface protein with similarity to human collagen (S. Lukomski, K. Nakashima, I. Abdi, V. J. Cipriano, R. M. Ireland, S. R. Reid, G. G. Adams, and J. M. Musser, Infect. Immun. 68:6542-6553, 2000). This streptococcal collagen-like protein (Scl) contains a long region of Gly-X-X motifs and was produced by serotype M1 GAS strains. In the present study, a second member of the scl gene family was identified and designated scl2. The Scl2 protein also has a collagen-like region, which in M1 strains is composed of 38 contiguous Gly-X-X triplet motifs. The scl2 gene was present in all 50 genetically diverse GAS strains studied. The Scl2 protein is highly polymorphic, and the number of Gly-X-X motifs in the 50 strains studied ranged from 31 in one serotype M1 strain to 79 in serotype M28 and M77 isolates. The scl1 and scl2 genes were simultaneously transcribed in the exponential phase, and the Scl proteins were also produced. Scl1 and Scl2 were identified in a cell-associated form and free in culture supernatants. Production of Scl1 is regulated by Mga, a positive transcriptional regulator that controls expression of several GAS virulence factors. In contrast, production of Scl2 is controlled at the level of translation by variation in the number of short-sequence pentanucleotide repeats (CAAAA) located immediately downstream of the GTG (Val) start codon. Control of protein production by this molecular mechanism has not been identified previously in GAS. Together, the data indicate that GAS simultaneously produces two extracellular human collagen-like proteins in a regulated fashion.

SUBMITTER: Lukomski S

PROVIDER: S-EPMC98079 | biostudies-literature | 2001 Mar

REPOSITORIES: biostudies-literature

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Identification and characterization of a second extracellular collagen-like protein made by group A Streptococcus: control of production at the level of translation.

Lukomski S S Nakashima K K Abdi I I Cipriano V J VJ Shelvin B J BJ Graviss E A EA Musser J M JM

Infection and immunity 20010301 3

A recent study found that group A Streptococcus (GAS) expresses a cell surface protein with similarity to human collagen (S. Lukomski, K. Nakashima, I. Abdi, V. J. Cipriano, R. M. Ireland, S. R. Reid, G. G. Adams, and J. M. Musser, Infect. Immun. 68:6542-6553, 2000). This streptococcal collagen-like protein (Scl) contains a long region of Gly-X-X motifs and was produced by serotype M1 GAS strains. In the present study, a second member of the scl gene family was identified and designated scl2. Th ...[more]

PMID: 11179350

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Project description:Export of macromolecules via extracellular membrane-derived vesicles (MVs) plays an important role in the biology of Gram-negative bacteria. Gram-positive bacteria have also recently been reported to produce MVs; however, the composition and mechanisms governing vesiculogenesis in Gram-positive bacteria remain undefined. Here, we describe MV production in the Gram-positive human pathogen group A streptococcus (GAS), the etiological agent of necrotizing fasciitis and streptococcal toxic shock syndrome. M1 serotype GAS isolates in culture exhibit MV structures both on the cell wall surface and in the near vicinity of bacterial cells. A comprehensive analysis of MV proteins identified both virulence-associated protein substrates of the general secretory pathway in addition to "anchorless surface proteins." Characteristic differences in the contents, distributions, and fatty acid compositions of specific lipids between MVs and GAS cell membrane were also observed. Furthermore, deep RNA sequencing of vesicular RNAs revealed that GAS MVs contained differentially abundant RNA species relative to bacterial cellular RNA. MV production by GAS strains varied in a manner dependent on an intact two-component system, CovRS, with MV production negatively regulated by the system. Modulation of MV production through CovRS was found to be independent of both GAS cysteine protease SpeB and capsule biosynthesis. Our data provide an explanation for GAS secretion of macromolecules, including RNAs, lipids, and proteins, and illustrate a regulatory mechanism coordinating this secretory response. Group A streptococcus (GAS) is a Gram-positive bacterial pathogen responsible for more than 500,000 deaths annually. Establishment of GAS infection is dependent on a suite of proteins exported via the general secretory pathway. Here, we show that GAS naturally produces extracellular vesicles with a unique lipid composition that are laden with proteins and RNAs. Interestingly, both virulence-associated proteins and RNA species were found to be differentially abundant in vesicles relative to the bacteria. Furthermore, we show that genetic disruption of the virulence-associated two-component regulator CovRS leads to an increase in vesicle production. This study comprehensively describes the protein, RNA, and lipid composition of GAS-secreted MVs and alludes to a regulatory system impacting this process.

Dataset Information

Identification and characterization of a second extracellular collagen-like protein made by group A Streptococcus: control of production at the level of translation.

Publications

Identification and characterization of a second extracellular collagen-like protein made by group A Streptococcus: control of production at the level of translation.

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