The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.
Bacterial proteins binding to the mammalian extracellular matrix
Abstract
Summary: Pathogenic bacteria frequently express surface proteins with affinity for components of the mammalian extracellular matrix, i.e. collagens, laminin, fibronectin or proteoglycans. This review summarizes our current knowledge on the mechanisms of bacterial adherence to extracellular matrices and on the biological significance of these interactions. The best‐characterized bacterial proteins active in these interactions are the mycobacterial fibronectin‐binding proteins, the fibronectin‐ and the collagen‐binding proteins of staphylococci and streptococci, specific enterobacterial fimbrial types, as well as the polymeric surface proteins YadA of yersinias and the A‐protein of Aeromonas. Some of these bacterial proteins are highly specific for an extracellular matrix protein, some are multifunctional and express binding activities towards a number of target proteins. The interactions can be based on a protein‐protein or on a protein‐carbohydrate interaction, or on a bridging mechanism mediated by a bivalent soluble target protein. Many of the interactions have also been demonstrated on tissue sections or in vivo, and adherence to the extracellular matrix has been shown to promote bacterial colonization of damaged tissues.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Fibronectin binding mediated by a novel class of surface organelles on Escherichia coll
Olsén, A., Jonsson, A., & Normark, S. (1989) · Nature · doi:10.1038/338652a0 · Cited by 593
Signäs, C., Raucci, G., Jönsson, K., Lindgren, P. E., Anantharamaiah, G. M., Höök, M., & Lindberg, M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.2.699 · Cited by 383
JÖNSSON, K., SIGNÄS, C., MÜLLER, H., & LINDBERG, M. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16468.x · Cited by 365
Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis
Collinson, S. K., Emödy, L., Müller, K. H., Trust, T. J., & Kay, W. W. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.15.4773-4781.1991 · Cited by 346
Bifunctional properties of lectins: lectins redefined
Barondes, S. H. (1988) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(88)90235-6 · Cited by 334
P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips
Kuehn, M. J., Heuser, J., Normark, S., & Hultgren, S. J. (1992) · Nature · doi:10.1038/356252a0 · Cited by 332
Patti, J. M., Jonsson, H., Guss, B., Switalski, L. M., Wiberg, K., Lindberg, M., & Höök, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42898-0 · Cited by 282
Olsén, A., Arnqvist, A., Hammar, M., Sukupolvi, S., & Normark, S. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01143.x · Cited by 282
Presence of Laminin Receptors in Staphylococcus aureus
Lopes, J. D., dos Reis, M., & Brentani, R. R. (1985) · Science · doi:10.1126/science.3160113 · Cited by 269
Abou-Zeid, C., Ratliff, T. L., Wiker, H. G., Harboe, M., Bennedsen, J., & Rook, G. A. (1988) · Infection and Immunity · doi:10.1128/iai.56.12.3046-3051.1988 · Cited by 265
Cited by
Navarre, W. W., & Schneewind, O. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.174-229.1999 · Cited by 1,391
Dramsi, S., Biswas, I., Maguin, E., Braun, L., Mastroeni, P., & Cossart, P. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.tb02297.x · Cited by 462
Mucosal Prevalence and Interactions with the Epithelium Indicate Commensalism of Sutterella spp.
Hiippala, K., Kainulainen, V., Kalliomäki, M., Arkkila, P., & Satokari, R. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01706 · Cited by 351
“ECM components, on the other hand, are located in the basal lamina providing support for the epithelial cells and exposed to the luminal bacteria only if the mucosal surface is disrupted (Westerlund and Korhonen, 1993).”
BackgroundSingh, B., Fleury, C., Jalalvand, F., & Riesbeck, K. (2012) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2012.00340.x · Cited by 302
Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells
Joh, D., Wann, E. R., Kreikemeyer, B., Speziale, P., & Höök, M. (1999) · Matrix Biology · doi:10.1016/s0945-053x(99)00025-6 · Cited by 278
Metadata
- Authors
- Westerlund, B., & Korhonen, T. K.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 1993-08
- Volume
- 9
- Issue
- 4
- Pages
- 687-694
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2147374678
- Cited by
- 313
- References
- 64
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Bacterial proteins binding to the mammalian extracellular matrix. https://app.cochat.ai/papers/10.1111/j.1365-2958.1993.tb01729.x
- The paper
- Westerlund, B., & Korhonen, T. K. (1993). Bacterial proteins binding to the mammalian extracellular matrix. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.1993.tb01729.x
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.