Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Coiled-Coil Irregularities and Instabilities in Group A <i>Streptococcus</i> M1 Are Required for Virulence

6 Mar 2008

Abstract excerpt

Antigenically variable M proteins are major virulence factors and immunogens of the human pathogen group A Streptococcus (GAS). Here, we report the approximately 3 angstrom resolution structure of a GAS M1 fragment containing the regions responsible for eliciting type-specific, protective immunity and for binding fibrinogen, which promotes M1 proinflammatory and antiphagocytic functions. The structure revealed...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antimicrobial Resistance in Staphylococcus
Share to Neonatal and Maternal Infections
Share to Streptococcal Infections and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 18323455
DOI: 10.1126/science.1154470

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Coiled-Coil Irregularities and Instabilities in Group A <i>Streptococcus</i> M1 Are Required for VirulencePMID 18323455Read ↗

Coiled-coil irregularities of the M1 protein structure promote M1–fibrinogen interaction and influence group A Streptococcus host cell interactions and virulenceSemantic proximity Read ↗

Coiled-coil destabilizing residues in the group A Streptococcus M1 protein are required for functional interaction.Semantic proximity Read ↗

Updated model of group A Streptococcus M proteins based on a comprehensive worldwide study.Semantic proximity Read ↗

Design of Broadly Cross-Reactive M Protein–Based Group A Streptococcal VaccinesSemantic proximity Read ↗

An M protein coiled coil unfurls and exposes its hydrophobic core to capture LL-37Semantic proximity Read ↗

A high-resolution cryo-EM structure of a bacterial M-protein reveals a compact structure that diverges from related M-proteinsSemantic proximity Read ↗

Structural basis for collagen recognition by the <i>Streptococcus pyogenes</i> M3 protein and its involvement in biofilmSemantic proximity Read ↗

The M protein of group A Streptococcus is a key virulence factor and a clinically relevant strain identification markerSemantic proximity Read ↗

The type-2 Streptococcus canis M protein SCM-2 binds fibrinogen and facilitates antiphagocytic propertiesSemantic proximity Read ↗

Group A Streptococcal S Protein Utilizes Red Blood Cells as Immune Camouflage and Is a Critical Determinant for Immune EvasionSemantic proximity Read ↗

The Crystal Structure of the Streptococcal Collagen-like Protein 2 Globular Domain from Invasive M3-type Group A Streptococcus Shows Significant Similarity to Immunomodulatory HIV Protein gp41Semantic proximity Read ↗

The increased hinge flexibility of an IgG1-IgG3 hybrid monoclonal enhances Fc-mediated protection against group A streptococciSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.