ArticleInfection and immunity2004
Truncation of fibronectin-binding proteins in Staphylococcus aureus strain Newman leads to deficient adherence and host cell invasion due to loss of the cell wall anchor function.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed, 157 citations in OpenAlex.
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- A Novel Interaction of Staphylococcal Protein A With Human Fibronectin and Its Implications in Host Cell Adhesion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
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- Protein Disulfide Isomerase and Extracellular Adherence Protein Cooperatively Potentiate Staphylococcal Invasion into Endothelial Cells.Microbiology spectrum · 2023Article
- All-Natural Immunomodulatory Bioadhesive Hydrogel Promotes Angiogenesis and Diabetic Wound Healing by Regulating Macrophage Heterogeneity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
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- Fibronectin binding protein B binds to loricrin and promotes corneocyte adhesion by Staphylococcus aureus.Nature communications · 2022Article
- Effect of Cobalt-Chromium-Molybdenum Implant Surface Modifications on Biofilm Development ofFrontiers in cellular and infection microbiology · 2022Article
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- Development and validation of a high-throughput whole cell assay to investigateThe Journal of biological chemistry · 2020Article
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- Staphylococcus aureus Fibronectin Binding Protein A Mediates Biofilm Development and Infection.Infection and immunity · 2020Article
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- Identification of surface proteins in a clinical Staphylococcus haemolyticus isolate by bacterial surface shaving.BMC microbiology · 2020Article
26 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus aureus fibronectin-binding proteins (FnBPs) play a critical role in S. aureus pathogenesis. FnBPs mediate adhesion to fibronectin and invasion of mammalian cells, including epithelial, endothelial, and fibroblastic cells, by fibronectin bridging to the host cell fibronectin receptor integrin (alpha(5))beta(1). Strain Newman is a laboratory strain frequently used for genetic, functional, and in vivo studies. However, despite pronounced production of FnBPs, strain Newman is only weakly adherent to immobilized Fn and weakly invasive. We examined whether these effects are due to a structural difference of FnBPs. Here, we show that both fnbA(Newman) and fnbB(Newman) contain a centrally located point mutation resulting in a stop codon. This leads to a truncation of both FnBPs at the end of the C domain at identical positions. Most likely, the stop codon occurred first in fnbB(Newman) and was subsequently transferred to fnbA(Newman) by replacement of the entire region encompassing the C, D, and W domains with the respective sequence of fnbB(Newman). Using heterologous expression in Staphylococcus carnosus, we found that truncated FnBPs were completely secreted into the culture medium and not anchored to the cell wall, since they lack the sortase motif (LPETG). Consequently, this led to a loss of FnBP-dependent functions, such as strong adhesion to immobilized fibronectin, binding of fibrinogen, and host cell invasion. This mutation may explain some of the earlier reported conflicting data with strain Newman. Thus, care should be taken when drawing negative conclusions about the role of FnBPs as a virulence factor in a given model.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.