Evolution of Streptococcus pyogenes has maximized the efficiency of the Sortase A cleavage motif for cell wall transpeptidation-Reference-Cited by-同舟云学术

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Evolution of Streptococcus pyogenes has maximized the efficiency of the Sortase A cleavage motif for cell wall transpeptidation

Published:2022-06 Issue:6 Volume:298 Page:101940
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Readnour Bradley M.,Ayinuola Yetunde A.,Russo Brady T.,Liang Zhong,Lee Shaun W.,Ploplis Victoria A.,Fischetti Vincent A.,Castellino Francis J.

Funder

NIH

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 articles.

1. M protein and other surface proteins on streptococci;Fischetti,2016

2. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity;Pancholi;J. Exp. Med.,1992

3. a-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci;Pancholi;J. Biol. Chem.,1998

4. The human pathogen Streptococcus pyogenes releases, lipoproteins as lipoprotein-rich membranevesicles;Biagini;Mol. Cell. Proteomics,2015

5. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci;Fischetti;Mol. Microbiol.,1990

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