Back to search

Article

A high-resolution cryo-EM structure of a bacterial M-protein reveals a compact structure that diverges from related M-proteins

2023-09-18

Abstract excerpt

The surface of Streptococcus pyogenes (GAS) is studded with virulence determinants, with the most abundant being the characteristic M-protein used to serotype various strains of the bacterium. There are >250 strains of GAS serotypically distinguished by their M-proteins. Major pathogenic mechanisms of GAS require that this microorganism hijacks host components for survival, many of which are involved in hemostasi...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
c692c4bf-11b4-5b2b-bf10-0f0cfe987bbd
DOI
10.1101/2023.09.18.558297
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
A high-resolution cryo-EM structure of a bacterial M-protein reveals a compact structure that diverges from related M-proteinsDOI 10.1101/2023.09.18.558297
Select a neighboring publication to make it the new centre.