Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host
Abstract
Laminin (Ln) and collagen are multifunctional glycoproteins that play an important role in cellular morphogenesis, cell signalling, tissue repair and cell migration. These proteins are ubiquitously present in tissues as a part of the basement membrane (BM), constitute a protective layer around blood capillaries and are included in the extracellular matrix (ECM). As a component of BMs, both Lns and collagen(s), thus function as major mechanical containment molecules that protect tissues from pathogens. Invasive pathogens breach the basal lamina and degrade ECM proteins of interstitial spaces and connective tissues using various ECM-degrading proteases or surface-bound plasminogen and matrix metalloproteinases recruited from the host. Most pathogens associated with the respiratory, gastrointestinal, or urogenital tracts, as well as with the central nervous system or the skin, have the capacity to bind and degrade Lns and collagen(s) in order to adhere to and invade host tissues. In this review, we focus on the adaptability of various pathogens to utilize these ECM proteins as enhancers for adhesion to host tissues or as a targets for degradation in order to breach the cellular barriers. The major pathogens discussed are Streptococcus, Staphylococcus, Pseudomonas, Salmonella, Yersinia, Treponema, Mycobacterium, Clostridium, Listeria, Porphyromonas and Haemophilus; Candida, Aspergillus, Pneumocystis, Cryptococcus and Coccidioides; Acanthamoeba, Trypanosoma and Trichomonas; retrovirus and papilloma virus.
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Fibroblasts sense pathogens and secrete inflammatory mediators.
“Fibroblasts, though non-hematopoietic, also sense pathogens and secrete inflammatory mediators, highlighting the skin’s integrated immune-stromal cell network (see section below) [34–36].”
From Host–Candida auris interactions in the skin (2026) · cites this paper as [35]
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Host–Candida auris interactions in the skin
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- Authors
- Singh, B., Fleury, C., Jalalvand, F., & Riesbeck, K.
- Affiliations
- Lund University (SE)
- Venue
- FEMS Microbiology Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 2012-11
- Volume
- 36
- Issue
- 6
- Pages
- 1122-1180
- ISSN
- 0168-6445 (ISSN-L)
- 1574-6976
- OpenAlex
- W2097910973
- Cited by
- 302
- References
- 14
- Citations by year
- 2026: 16 · 2025: 24 · 2024: 27 · 2023: 25 · 2022: 35 · 2021: 26 · 2020: 23 · 2019: 19 · 2018: 26 · 2017: 18 · 2016: 21 · 2015: 13 · 2014: 17 · 2013: 8 · 2012: 4
- FWCI
- 1.84
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEMS Microbiology Reviews (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- laminin, collagen, extracellular matrix, bacterial adhesion, bacterial invasion, basement membrane, matrix metalloproteinases, plasminogen, extracellular matrix degradation, host-pathogen interaction, Streptococcus, Staphylococcus, Pseudomonas, Salmonella, Yersinia, Treponema, Mycobacterium, Clostridium, Listeria, Porphyromonas, Haemophilus, Candida, Aspergillus, Pneumocystis, Cryptococcus, Coccidioides, Acanthamoeba, trypanosomes, Trichomonas, retroviruses, papillomavirus
- MeSH terms
- Bacteria, Bacterial Adhesion, Collagen, Communicable Diseases, Fungi, Humans, Laminin, Parasitic Diseases, Host-Pathogen Interactions
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