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

Scl1‐dependent internalization of group A Streptococcus via direct interactions with the α2β1 integrin enhances pathogen survival and re‐emergence

30 May 2007

Abstract excerpt

The molecular pathogenesis of infections caused by group A Streptococcus (GAS) is not fully understood. We recently reported that a recombinant protein derived from the collagen-like surface protein, Scl1, bound to the human collagen receptor, integrin alpha(2)beta(1). Here, we investigate whether the same Scl1 variant expressed by GAS cells interacts with the integrin alpha2beta(1) and affects the biological...

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: 17542923
DOI: 10.1111/j.1365-2958.2007.05741.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Scl1‐dependent internalization of group A Streptococcus via direct interactions with the α2β1 integrin enhances pathogen survival and re‐emergencePMID 17542923Read ↗

Scl1, the multifunctional adhesin of group A<i>Streptococcus</i>, selectively binds cellular fibronectin and laminin, and mediates pathogen internalization by human cellsSemantic proximity Read ↗

Natural variant of collagen-like protein a in serotype M3 group a Streptococcus increases adherence and decreases invasive potential.Semantic proximity Read ↗

Adaptation of the group A Streptococcus adhesin Scl1 to bind fibronectin type III repeats within wound‐associated extracellular matrix: implications for cancer therapySemantic proximity Read ↗

The streptococcal collagen-like protein-1 (Scl1) is a significant determinant for biofilm formation by group a StreptococcusSemantic proximity Read ↗

The group A streptococcal collagen‐like protein‐1, Scl1 , mediates biofilm formation by targeting the extra domain A ‐containing variant of cellular fibronectin expressed in wounded tissueSemantic proximity Read ↗

Identification and characterization of the scl gene encoding a group A Streptococcus extracellular protein virulence factor with similarity to human collagen.Semantic proximity Read ↗

Integrin-linked kinase is an essential link between integrins and uptake of bacterial pathogens by epithelial cells.Semantic proximity Read ↗

Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1Semantic proximity Read ↗

Binding of the low‐density lipoprotein by streptococcal collagen‐like protein Scl1 of <i>Streptococcus pyogenes</i>Semantic proximity Read ↗

The Surface Protein Srr-1 of Streptococcus agalactiae Binds Human Keratin 4 and Promotes Adherence to Epithelial HEp-2 CellsSemantic proximity Read ↗

Three glycosylated serine‐rich repeat proteins play a pivotal role in adhesion and colonization of the pioneer commensal bacterium, Streptococcus salivariusSemantic proximity Read ↗

Roles of integrins and fibronectin in the entry of <i>Streptococcus pyogenes</i> into cells via protein F1Semantic proximity Read ↗

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