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Lactobacilli express cell surface proteins which mediate binding of immobilized collagen and fibronectin

Lorca, G; Torino, MI; de Valdez, GF and Ljungh, Åsa LU (2002) In FEMS Microbiology Letters 206(1). p.31-37
Abstract
Binding of immobilized collagen-I (Cn-I) and fibronectin (Fn) by Lactobacillus acidophilus CRL 639 depends on cell-surface proteins. Capsule formation during the stationary growth phase has a negative effect on adherence of Cn-I and Fn. However, cells from the exponential growth phase. which produce no capsule, exhibit maximal binding. Binding is sensitive to trypsin, proteinase K, pronase E, and heat. Gelatin and soluble Cn-I partially inhibit binding of Cn-I although various proteins, sugars and amino acids do not affect binding to Fn. These results indicate that protein-protein interactions mediate adhesion to extracellular matrix proteins. SDS-PAGE and Western blot analyses of surface proteins revealed that several proteins including... (More)
Binding of immobilized collagen-I (Cn-I) and fibronectin (Fn) by Lactobacillus acidophilus CRL 639 depends on cell-surface proteins. Capsule formation during the stationary growth phase has a negative effect on adherence of Cn-I and Fn. However, cells from the exponential growth phase. which produce no capsule, exhibit maximal binding. Binding is sensitive to trypsin, proteinase K, pronase E, and heat. Gelatin and soluble Cn-I partially inhibit binding of Cn-I although various proteins, sugars and amino acids do not affect binding to Fn. These results indicate that protein-protein interactions mediate adhesion to extracellular matrix proteins. SDS-PAGE and Western blot analyses of surface proteins revealed that several proteins including the major 43-kDa protein of the S-layer are expressed. Monoclonal antibodies showed that Fn binds to a 15-kDa protein, while Cn-I binds to proteins of 45 and 58 kDa. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
immunoblot, polysaccharide, fibronectin binding, Lactobacillus, collagen binding, protein-protein interaction
in
FEMS Microbiology Letters
volume
206
issue
1
pages
31 - 37
publisher
Elsevier
external identifiers
  • wos:000173284600005
  • pmid:11786253
  • scopus:0037005874
ISSN
1574-6968
DOI
10.1016/S0378-1097(01)00512-2
language
English
LU publication?
yes
id
855c067c-6d6c-4d37-8cfd-18fda462d29f (old id 345903)
date added to LUP
2007-11-02 09:44:23
date last changed
2017-12-10 04:32:04
@article{855c067c-6d6c-4d37-8cfd-18fda462d29f,
  abstract     = {Binding of immobilized collagen-I (Cn-I) and fibronectin (Fn) by Lactobacillus acidophilus CRL 639 depends on cell-surface proteins. Capsule formation during the stationary growth phase has a negative effect on adherence of Cn-I and Fn. However, cells from the exponential growth phase. which produce no capsule, exhibit maximal binding. Binding is sensitive to trypsin, proteinase K, pronase E, and heat. Gelatin and soluble Cn-I partially inhibit binding of Cn-I although various proteins, sugars and amino acids do not affect binding to Fn. These results indicate that protein-protein interactions mediate adhesion to extracellular matrix proteins. SDS-PAGE and Western blot analyses of surface proteins revealed that several proteins including the major 43-kDa protein of the S-layer are expressed. Monoclonal antibodies showed that Fn binds to a 15-kDa protein, while Cn-I binds to proteins of 45 and 58 kDa.},
  author       = {Lorca, G and Torino, MI and de Valdez, GF and Ljungh, Åsa},
  issn         = {1574-6968},
  keyword      = {immunoblot,polysaccharide,fibronectin binding,Lactobacillus,collagen binding,protein-protein interaction},
  language     = {eng},
  number       = {1},
  pages        = {31--37},
  publisher    = {Elsevier},
  series       = {FEMS Microbiology Letters},
  title        = {Lactobacilli express cell surface proteins which mediate binding of immobilized collagen and fibronectin},
  url          = {http://dx.doi.org/10.1016/S0378-1097(01)00512-2},
  volume       = {206},
  year         = {2002},
}