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

The antibacterial activity of peptides derived from human beta‐2 glycoprotein I is inhibited by protein H and M1 protein from <i>Streptococcus pyogenes</i>

17 Oct 2007

Abstract excerpt

During the last years, the importance of antibacterial peptides has attracted considerable attention. We report here that peptides derived from the fifth domain of beta-2 glycoprotein I (beta(2)GPI), a human heparin binding plasma protein, have antibacterial activities against Gram-positive and Gram-negative bacteria. Streptococcus pyogenes, an important human pathogen that can survive and grow in human blood,...

Read the complete abstract on PubMed

Topics

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

Share to Antimicrobial Peptides and Activities
Share to Biochemical and Structural Characterization
Share to Streptococcal Infections and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 18093092
DOI: 10.1111/j.1365-2958.2007.05974.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The antibacterial activity of peptides derived from human beta‐2 glycoprotein I is inhibited by protein H and M1 protein from <i>Streptococcus pyogenes</i>PMID 18093092Read ↗

Binding of complement inhibitor C4b-binding protein to a highly virulent Streptococcus pyogenes M1 strain is mediated by protein H and enhances adhesion to and invasion of endothelial cells.Semantic proximity Read ↗

Interactions between M proteins of <i>Streptococcus pyogenes</i> and glycosaminoglycans promote bacterial adhesion to host cellsSemantic proximity Read ↗

Distinct Serotypes of Streptococcal M Proteins Mediate Fibrinogen-Dependent Platelet Activation and Proinflammatory EffectsSemantic proximity Read ↗

Virulent aggregates of <i>Streptococcus pyogenes</i> are generated by homophilic protein–protein interactionsSemantic proximity Read ↗

M1 protein and protein H: IgGFc- and albumin-binding streptococcal surface proteins encoded by adjacent genesSemantic proximity Read ↗

The <i>Streptococcus pyogenes</i> M protein is involved in phenotypic resistance to phage A25 infection in presence of human serumSemantic proximity Read ↗

Protein GRAB of streptococcus pyogenes regulates proteolysis at the bacterial surface by binding alpha2-macroglobulin.Semantic proximity Read ↗

Evasion of Phagocytosis through Cooperation between Two Ligand-binding Regions in <i>Streptococcus pyogenes</i> M ProteinSemantic proximity Read ↗

Human fibrinogen bound to Streptococcus pyogenes M protein inhibits complement deposition via the classical pathwaySemantic proximity Read ↗

Ig-binding surface proteins of Streptococcus pyogenes also bind human C4b-binding protein (C4BP), a regulatory component of the complement system.Semantic proximity Read ↗

Streptococcal M Protein: A Multipotent and Powerful Inducer of InflammationSemantic proximity Read ↗

The group B streptococcal beta and pneumococcal Hic proteins are structurally related immune evasion molecules that bind the complement inhibitor factor H in an analogous fashion.Semantic proximity Read ↗

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