Hostname: page-component-78c5997874-m6dg7 Total loading time: 0 Render date: 2024-11-15T01:59:56.252Z Has data issue: false hasContentIssue false
  • English
  • Français

Cell surface hydrophobicity and adherence to extra–cellular matrix proteins in two collections of methicillin–resistant Staphylococcus aureus

Published online by Cambridge University Press:  15 May 2009

R. G. A. Cree ,
P. Aleljung ,
M. Paulsson ,
W. Witte ,
W. C. Noble ,
A. Ljungh  and
T. Wadström
R. G. A. Cree
Affiliation:
Department of Microbial Diseases, St John's Institute of Dermatology, St Thomas' Hospital, London SE1 7EH, UK
P. Aleljung
Affiliation:
Department of Medical Microbiology, Lund University, S-223 63, Lund, Sweden
M. Paulsson
Affiliation:
Department of Medical Microbiology, Lund University, S-223 63, Lund, Sweden
W. Witte
Affiliation:
Bundesgesundheitsamt, Robert von Ostertag Institut, Bereich Wernigerode D-0-3700 Wernigerode, Germany
W. C. Noble*
Affiliation:
Department of Microbial Diseases, St John's Institute of Dermatology, St Thomas' Hospital, London SE1 7EH, UK
A. Ljungh
Affiliation:
Department of Medical Microbiology, Lund University, S-223 63, Lund, Sweden
T. Wadström
Affiliation:
Department of Medical Microbiology, Lund University, S-223 63, Lund, Sweden
*
*Professor W.C.Noble, Department of Microbial Diseases. St John's Institute of Dermatology. St Thomas' Hospital. London SE1 7EH
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Non-specific and specific mechanisms of adherence have been examined in two collections of methicillin–resistant Staphylococcus aureus (MRSA). Determination of hydrophobicity by salt aggregation, hydrophobicity indices and of adherence to the extra–cellular matrix proteins fibronectin, vitronectin, laminin and collagen type 1 have failed to reveal any correlation with phage-type, plasmid profile or antibiogram. Further, the strain collections, made over a period of years in two countries, differ markedly in their adherence characteristics; MRSA are heterogeneous in this respect. Such heterogeneity may explain the polarization of views on the epidemicity or ‘virulence’ of MRSA. With the exception of adherence to collagen a small group of methicillin sensitive S. aureus had characteristics intermediate between the two groups of MRSA.

Type
Research Article
Information
Epidemiology & Infection , Volume 112 , Issue 2 , April 1994 , pp. 307 - 314
Copyright
Copyright © Cambridge University Press 1994

References

REFERENCES

Casewell, MW, Hill, RLR. The carrier state: methicillin-resistant Staphylococcus aureus. J Antimicrob Chemother 1986; 18 Suppl A: 1–12.CrossRefGoogle ScholarPubMed
Keane, CT, Cafferkey, MT. Methicillin–resistant Staphylococcus aureus: a guide to epidemiology and control. Rev Microbiol 1991; 2: 50–6.Google Scholar
Lacey, RW, Barr, KW, Barr, VE, Inglis, TT. Properties of methicillin–resistant Staphylococcus aureus colonizing patients in a burns unit. J Hosp Infect 1986; 7: 137–48.CrossRefGoogle Scholar
Lentino, JR, Hennein, H, Krause, S et al. , A comparison of pneumonia caused by gentamicin, methicillin–resistant and gentamicin, methicillin–sensitive Staphylococcus aureus: epidemiology and clinical studies. Infect Control 1985; 6: 267–72.CrossRefGoogle ScholarPubMed
Kreiswirth, B, Kornblum, J, Arbeit, RD et al. , Evidence for a clonal origin of methicillin–resistance in Staphylococcus aureus. Science 1993; 259: 227–30.CrossRefGoogle ScholarPubMed
Beachy, H. Bacterial adherence: adhesin receptor interaction mediating the attachment of bacteria to mucosal surfaces. J Infect Dis 1981; 143: 325–44.CrossRefGoogle Scholar
Naidu, AS, Paulsson, M, Wadström, T. Particle agglutination assays for rapid detection of fibronectin, fibrinogen and collagen receptors on Staphylococcus aureus. J Clin Microbiol 1988; 26: 1549–54.CrossRefGoogle ScholarPubMed
Herrmann, M, Vaudaux, PE, Pittet, D et al. , Fibronectin, fibronogen and laminin act as mediators of adherence of clinical staphylococcal isolates to foreign material. J Infect Dis 1988; 158: 693–701.CrossRefGoogle Scholar
Kuusela, P, Vartio, T, Vuento, M, Myhre, EB. Attachment of staphylococci and steptococci on fibronectin, fibronectin fragments and fibrinogen bound to a solid phase. Infect Immun 1985; 50: 77–81.CrossRefGoogle Scholar
Proctor, RH. The staphylococcal fibronectin receptor: evidence for its importance in invasive infections. Rev Infect Dis 1987; 9 Suppl 4: S335–40.CrossRefGoogle ScholarPubMed
Toy, PTCY, Lai, L-W, Drake, TA, Sande, MA. Effect of fibronectin on adherence of Staphylococcus aureus to fibrin thrombi in vitro. Infect Immun 1985; 48: 83–6.CrossRefGoogle ScholarPubMed
Chatwal, GS, Preissner, KT, Muller-Berghaus, G, Blobel, H. Specific binding of the human S protein (vitronectin) to streptococci, Staphylococcus aureus and Escherichia coli. Infect Immun 1987; 55: 1878–83.CrossRefGoogle Scholar
Paulsson, M, Laing, OD, Ascencio, F, Wadström, T. Vitronectin–binding surface proteins of Staphylococcus aureus. Zbl Bakt 1992; 277: 54–64.CrossRefGoogle ScholarPubMed
Smyth, CJ, Jonsson, P, Olsson, E, Soderlind, O, Rosengren, J, Hjerten, S, Wadström, T. Differences in hydrophobic surface characteristics of porcine enteropathogenic Escherichia coli with and without K88 antigen as revealed by hydrophobic interaction chromatography. Infect Immun 1978; 22: 462–72.CrossRefGoogle ScholarPubMed
Lindhal, M, Faris, A, Wadström, T, Hjerten, S. A new test based on “salting out” to measure relative surface hydrophobicity of bacterial cells. Biochim Biophys Acta 1981; 77: 471–6.CrossRefGoogle Scholar
Ljungh, A, Hjerten, S, Wadström, T. High surface hydrophobicity of autoagglutinating Staphylococcus aureus strains isolated from human infections studied with the salt aggregation test. Infect Immun 1985; 47: 522–76.CrossRefGoogle Scholar
Vuento, M, Vaheri, A. Purification of fibronectin from human plasma by affinity chromatography under non–denaturing conditions. Biochem J 1979; 183: 331–7.CrossRefGoogle ScholarPubMed
Valkonon, KH, Veljola, A, Dagberg, B, Uhlin, BE. Binding of basement membrane laminin by Escherichia coli. Mol Microbiol 1991; 5: 2133–41.CrossRefGoogle Scholar
Yatohgo, T, Izvmi, M, Kashiwagi, H, Hayashi, M. Novel purification of vitronectin from human plasma by heparin affinity chromatography. Cell Struct Funct 1988; 13: 281–92.CrossRefGoogle ScholarPubMed
Costas, M, Cookson, BDTalsania, HG, Owen, RJ. Numerical analysis of electrophoresis protein patterns of methicillin–resistant strains of Staphylococcus aureus. J Clin Microbiol 1984; 27: 2574–81.CrossRefGoogle Scholar
Prevost, G, Jauhac, B, Piemont, Y. DNA fingerprinting by pulsed field gel electrophoresis is more effective than ribotyping in distinguishing among methicillin-resistant Staphylococcus aureus. J Clin Microbiol 1992; 30: 967–73.CrossRefGoogle ScholarPubMed
Wei, M-Q, Groth, DM, Mendis, AHW, Sampson, J, Wetherall, JD, Grubb, WB. Typing of methicillin–resistant Staphylococcus aureus with an M13 repeat probe. J Hosp Infect 1992; 20: 233–5.CrossRefGoogle ScholarPubMed
Zuccarelli, AJ, Roy, I, Harding, GP, Couperus, JJ. Diversity and stability of restriction enzyme profiles of plasmid DNA from methicillin–resistant Staphylococcus aureus. J Clin Microbiol 1990; 28: 97–102.CrossRefGoogle ScholarPubMed