Cited by 1,191Biochemical and Structural CharacterizationAntimicrobial Resistance in StaphylococcusBacterial biofilms and quorum sensing

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MSCRAMM-MEDIATED ADHERENCE OF MICROORGANISMS TO HOST TISSUES

Patti, Joseph M., Allen, Bradley L., McGavin, Martin J., Höök, Magnus·1994·Annual Review of Microbiology

DOI 10.1146/annurev.mi.48.100194.003101

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Abstract

Microbial adhesion to host tissue is the initial critical event in the pathogenesis of most infections and, as such, is an attractive target for the development of new antimicrobial therapeutics. Specific microbial components (adhesins) mediate adherence to host tissues by participating in amazingly sophisticated interactions with host molecules. This review focuses on a class of cell surface adhesins that specifically interact with extracellular matrix components and which we have designated MSCRAMMs (microbial surface components recognizing adhesive matrix molecules). MSCRAMMs recognizing fibronectin-, fibrinogen-, collagen-, and heparin-related polysaccharides are discussed in terms of structural organization, ligand-binding structures, importance in host tissue colonization and invasion, and role as virulence factors.

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Bacterial Adherence: Adhesin-Receptor Interactions Mediating the Attachment of Bacteria to Mucosal Surfaces
Beachey, E. H. (1981) · Journal of Infectious Diseases · doi:10.1093/infdis/143.3.325 · Cited by 1,411
Multiple β1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells
Isberg, R. R., & Leong, J. M. (1990) · Cell · doi:10.1016/0092-8674(90)90099-z · Cited by 798
Fibronectin binding mediated by a novel class of surface organelles on Escherichia coll
Olsén, A., Jonsson, A., & Normark, S. J. (1989) · Nature · doi:10.1038/338652a0 · Cited by 614
Identification of invasin: A protein that allows enteric bacteria to penetrate cultured mammalian cells
Isberg, R. R., Voorhis, D. L., & Falkow, S. (1987) · Cell · doi:10.1016/0092-8674(87)90335-7 · Cited by 597
Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane.
Liotta, L. A., Goldfarb, R. H., Brundage, R. A., Siegal, G. P., Terranova, V. P., & Garbisa, S. (1981) · PubMed · Cited by 597
Fibronectin binds to Staphylococcus aureus
Kuusela, P. (1978) · Nature · doi:10.1038/276718a0 · Cited by 457
Conservation of a hexapeptide sequence in the anchor region of surface proteins from Gram‐positive cocci
Fischetti, V. A., Pancholi, V., & Schneewind, O. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb02072.x · Cited by 411
Serotypes, hemolysin production, and receptor recognition of Escherichia coli strains associated with neonatal sepsis and meningitis
Korhonen, T. K., Valtonen, M., Parkkinen, J., Väisänen-Rhen, V., Finne, J., Ørskov, F., Ørskov, I., Svenson, S. B., & Mäkelä, P. H. (1985) · Infection and Immunity · doi:10.1128/iai.48.2.486-491.1985 · Cited by 360
Malaria circumsporozoite protein binds to heparan sulfate proteoglycans associated with the surface membrane of hepatocytes.
Frevert, U., Sinnis, P., Cerami, C., Shreffler, W. G., Takács, B., & Nussenzweig, V. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.5.1287 · Cited by 351
Antibodies to the conserved cytoplasmic domain of the integrin beta 1 subunit react with proteins in vertebrates, invertebrates, and fungi.
Marcantonio, E. E., & Hynes, R. O. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.106.5.1765 · Cited by 319

Show all 83 references

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Snodgrass, J. L., Mohamed, N., Ross, J., Sau, S., Lee, C. Y., & Smeltzer, M. S. (1999) · Infection and Immunity · doi:10.1128/iai.67.8.3952-3959.1999 · Cited by 34
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Lo, Y.-Y., Hsu, S., Ko, Y.-C., Hung, C., Chang, M., Hsu, H., Pan, M.-J., Chen, Y.-W., Lee, C., Tseng, F., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.418699 · Cited by 34
Genetic Mechanisms Underlying the Pathogenicity of Cold-Stressed Salmonella enterica Serovar Typhimurium in Cultured Intestinal Epithelial Cells
Shah, J., Desai, P., & Weimer, B. C. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.01994-14 · Cited by 34
The role of hypervirulent Staphylococcus aureus infections in the development of deep vein thrombosis
Martin, E., Çevik, C., & NUGENT, K. M. (2012) · Thrombosis Research · doi:10.1016/j.thromres.2012.06.013 · Cited by 36
Identification of a polymorphic collagen-like protein in the crustacean bacteria Pasteuria ramosa
Mouton, L., Traunecker, E., McElroy, K., Pasquier, L. D., & Ebert, D. (2009) · Research in Microbiology · doi:10.1016/j.resmic.2009.08.016 · Cited by 34
In Vitro Models That Support Adhesion Specificity in Biofilms of Oral Bacteria
Ellen, R. P., Lépine, G., & Nghiem, P.-M. (1997) · Advances in Dental Research · doi:10.1177/08959374970110011401 · Cited by 34
Tissue-Specific Adherent Enterococcus faecalis Strains That Show Highly Efficient Adhesion to Human Bladder Carcinoma T24 Cells Also Adhere to Extracellular Matrix Proteins
Tomita, H., & Ike, Y. (2004) · Infection and Immunity · doi:10.1128/iai.72.10.5877-5885.2004 · Cited by 34
Inhibition of Staphylococcal Wound Infection and Potentiation of Antibiotic Prophylaxis by a Recombinant Fragment of the Fibronectin‐Binding Protein ofStaphylococcus aureus
Menzies, B. E., Kourteva, Y., Kaiser, A. B., & Kernodle, D. S. (2002) · The Journal of Infectious Diseases · doi:10.1086/339484 · Cited by 34
Ail Protein Binds Ninth Type III Fibronectin Repeat (9FNIII) within Central 120-kDa Region of Fibronectin to Facilitate Cell Binding by Yersinia pestis
Tsang, T. M., Annis, D. S., Kronshage, M., Fenno, J. T., Usselman, L. D., Mosher, D. F., & Krukonis, E. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.358978 · Cited by 33
Assessment of the Dual Role of Clumping Factor A in S. Aureus Adhesion to Endothelium in Absence and Presence of Plasma
Claes, J., Ditkowski, B., Liesenborghs, L., Veloso, T. R., Entenza, J. M., Moreillon, P., Vanassche, T., Verhamme, P. B., Hoylaerts, M., & Heying, R. (2018) · Thrombosis and Haemostasis · doi:10.1055/s-0038-1660435 · Cited by 32
Bacterial Adhesion and Biomaterial Surfaces
Moriarty, T. F., Poulsson, A. H. C., Rochford, E. T. J., & Richards, R. G. (2011) · Elsevier eBooks · doi:10.1016/b978-0-08-055294-1.00007-6 · Cited by 34
Staphylococcal Factors Involved in Adhesion and Biofilm Formation on Biomaterials
Mack, D., Bartscht, K., Dobinsky, S., Horstkotte, M. A., Kiel, K., Knobloch, J. K. ‐., & Schafer, P. H. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-224-1_20 · Cited by 33
Mammalian Cell-Based Sensor System
Banerjee, P., Franz, B., & Bhunia, A. K. (2010) · Springer eBooks · doi:10.1007/10_2009_21 · Cited by 33
Transcriptional regulation of the Staphylococcus aureus collagen adhesion gene, cna
Gillaspy, A. F., Patti, J. M., & Smeltzer, M. S. (1997) · Infection and Immunity · doi:10.1128/iai.65.4.1536-1540.1997 · Cited by 33
Self-citation
Solution Structure of the N-Terminal F1 Module Pair from Human Fibronectin,
Potts, J. R., Bright, J. R., Bolton, D., Pickford, A. R., & Campbell, I. D. (1999) · Biochemistry · doi:10.1021/bi990202b · Cited by 33
Fructose-1,6-bisphosphate aldolase is involved in Mycoplasma bovis colonization as a fibronectin-binding adhesin
Huang, J., Zhu, H., Wang, J., Guo, Y., Ye, Z., Wei, H., Li, H., Guo, A., Liu, D., & Chen, X. (2019) · Research in Veterinary Science · doi:10.1016/j.rvsc.2019.02.010 · Cited by 32
A synergistic association between adhesion-related genes and multidrug resistance patterns of Staphylococcus aureus isolates from different patients and healthy individuals
Parastan, R., Kargar, M., Solhjoo, K., & Kafilzadeh, F. (2020) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2020.02.025 · Cited by 32
Bacterial attachment to immobilized extracellular matrix proteins in vitro
Zulfakar, S. S., White, J. D., Ross, T., & Tamplin, M. L. (2012) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2012.05.007 · Cited by 31
The modulation of extracellular superoxide dismutase in the specifically enhanced cellular immune response against secondary challenge of Vibrio splendidus in Pacific oyster (Crassostrea gigas)
Liu, C., Zhang, T., Wang, L., Wang, M., Wang, W., Jia, Z., Jiang, S., & Song, L. (2016) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2016.06.002 · Cited by 30
Genetics, Structure, and Function of Group A Streptococcal Pili
Nakata, M., & Kreikemeyer, B. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.616508 · Cited by 32
Potential factors involved in the early pathogenesis of Streptococcus uberis mastitis: a review
Fessia, A. S., & Odierno, L. M. (2021) · Folia Microbiologica · doi:10.1007/s12223-021-00879-9 · Cited by 30
Molecular basis of florfenicol-induced increase in adherence of Staphylococcus aureus strain Newman
Blickwede, M., Goethe, R., Wolz, C., Valentin‐Weigand, P., & Schwarz, Š. (2005) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dki233 · Cited by 31
Pathogenic Potential of Campylobacter ureolyticus
Burgos-Portugal, J. A., Kaakoush, N. O., Raftery, M. J., & Mitchell, H. M. (2011) · Infection and Immunity · doi:10.1128/iai.06031-11 · Cited by 31
An Integron Cassette Carrying dfr1 with 90-bp Repeat Sequences Located on the Chromosome of Trimethoprim-Resistant Isolates of Campylobacter jejuni
Gibreel, A., & Sköld, O. (2000) · Microbial Drug Resistance · doi:10.1089/107662900419384 · Cited by 31
The Surface Protein SdrF Mediates Staphylococcus epidermidis Adherence to Keratin
Trivedi, S., Uhlemann, A., Herman‐Bausier, P., Sullivan, S. B., Sowash, M. G., Flores, E. Y., Khan, S. D., Dufrêne, Y. F., & Lowy, F. D. (2017) · The Journal of Infectious Diseases · doi:10.1093/infdis/jix213 · Cited by 30

Authors: Patti, J. M., Allen, B. L., McGavin, M. J., & Höök, M.
Affiliations: Texas A&M University (US)
ORCID: Allen, Bradley L.
McGavin, Martin J.
Höök, Magnus
Venue: Annual Review of Microbiology
Publisher: Annual Reviews
Published: 1994-10
Volume: 48
Issue: 1
Pages: 585-617
ISSN: 0066-4227 (ISSN-L)
1545-3251
DOI: 10.1146/annurev.mi.48.100194.003101
OpenAlex: W2176472482
Cited by: 1,191
References: 83
Citations by year: 2026: 11 · 2025: 18 · 2024: 32 · 2023: 20 · 2022: 19 · 2021: 29 · 2020: 40 · 2019: 32 · 2018: 23 · 2017: 36 · 2016: 36 · 2015: 40 · 2014: 64 · 2013: 51 · 2012: 56
FWCI: 6.02
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Microbiology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01hl047313-03)
National Heart, Lung, and Blood Institute (HL 47313)
National Institute of Allergy and Infectious Diseases (AI20624)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
Keywords: MSCRAMMs, microbial adhesion, extracellular matrix, adhesins, fibronectin, fibrinogen, collagen, heparin, ligand binding, virulence factors, host-pathogen interaction, antimicrobial agents
MeSH terms: Amino Acid Sequence, Bacterial Adhesion, Gram-Negative Bacteria, Gram-Positive Bacteria, Heparin, Molecular Sequence Data, Extracellular Matrix Proteins, Adhesins, Bacterial

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