The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
The molecular basis of fibronectin‐mediated bacterial adherence to host cells
Open accessAbstract
Summary: Many pathogenic Gram‐positive bacteria produce cell wall‐anchored proteins that bind to components of the extracellular matrix (ECM) of the host. These bacterial MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) are thought to play a critical role in infection. One group of MSCRAMMs, produced by staphylococci and streptococci, targets fibronectin (Fn, a glycoprotein found in the ECM and body fluids of vertebrates) using repeats in the C‐terminal region of the bacterial protein. These bacterial Fn‐binding proteins (FnBPs) mediate adhesion to host tissue and bacterial uptake into non‐phagocytic host cells. Recent studies on interactions between the host and bacterial proteins at the residue‐specific level and on the mechanism of host cell invasion are providing a much clearer picture of these processes.
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Cites
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Cited by
Adhesion, invasion and evasion: the many functions of the surface proteins of Staphylococcus aureus
Foster, T. J., Geoghegan, J. A., Ganesh, V. K., & Höök, M. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3161 · Cited by 1,533
Self-citationLeptospira as an Emerging Pathogen: A Review of its Biology, Pathogenesis and Host Immune Responses
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Fibronectin: Molecular Structure, Fibrillar Structure and Mechanochemical Signaling
Dalton, C. J., & Lemmon, C. A. (2021) · Cells · doi:10.3390/cells10092443 · Cited by 319
Surface Adhesins of Staphylococcus aureus
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Molecular pathogenesis of neonatal group B streptococcal infection: no longer in its infancy
Doran, K. S., & Nizet, V. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04266.x · Cited by 219
Metadata
- Authors
- Schwarz‐Linek, U., Höök, M., & Potts, J. R.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2004-03-30
- Volume
- 52
- Issue
- 3
- Pages
- 631-641
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W1533381682
- Cited by
- 265
- References
- 68
- FWCI
- 6.67
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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