A Streptococcal Collagen-like Protein Interacts with the α2β1 Integrin and Induces Intracellular Signaling*
By J. Humtsoe, J. Kim, Yi Xu, D. Keene, M. Höök, S. Lukomski, K. Wary. Journal of Biological Chemistry, 2005
112 citations recorded by the source corpus.
The streptococcal collagen-like proteins Scl1 and Scl2 are prokaryotic members of a large protein family with domains containing the repeating amino acid sequence (Gly-Xaa-Yaa)n that form a collagen-like triple-helical structure. Here, we test the hypothesis that Scl variant might interact with mammalian collagen-binding integrins. We show that the recombinant Scl protein p176 promotes adhesion and spreading of human lung fibroblast cells through an α2β1 integrin-mediated interaction as shown in cell adhesion inhibition assays using anti-α2β1 and anti-β1 integrins monoclonal antibodies. Accordingly, C2C12 cells stably expressing α2β1 integrin as the only collagen-binding integrin show productive cell adhesion activities on p176 that can be blocked by an anti-α2β1 integrin antibody. In addition, p176 promotes tyrosine phosphorylation of p125FAK of C2C12 cells expressing α2β1 integrin, whereas parental cells do not. Furthermore, C2C12 adhesion of human lung fibroblast cells to p176 induces phosphorylation of p125FAK, p130CAS, and p68Paxillin proteins. In a domain swapping experiment, we show that integrin binds to the collagenous domain of the Scl protein. Moreover, the recombinant inserted domain of the α2 integrin interacts with p176 with a relatively high affinity (KD = 17 nm). Attempts to identify the integrin sites in p176 suggest that more than one site may be involved. These studies, for the first time, suggest that the collagen-like proteins of prokaryotes retained not only structural but also functional characteristics of their eukaryotic counterparts.
Subfields: Immunology and Allergy, Molecular Biology, Public Health, Environmental and Occupational Health
View Paper: https://www.semanticscholar.org/paper/2c01e8e8d6f160869c08d675b0636925f58caa7f
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
In Public Health, Environmental and Occupational Health
Citations in the corpus
- Streptococcus Adherence and Colonization (2009, background): “The collagen-like region has the functional properties of human collagen, interacting with 2 1 integrin and activating intracellular signaling pathways (248).”