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

Authors

  • Graciela Lorca,

    Corresponding author
    1. Centro de Referencia para Lactobacilos (CERELA, CONICET), Chacabuco 145, 4000 S.M. Tucumán, Argentina
    2. Department of Medical Microbiology, Dermatology and Infection, University of Lund, Sölvegatan 23, S-223 62 Lund, Sweden
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  • Marı́a Inés Torino,

    1. Centro de Referencia para Lactobacilos (CERELA, CONICET), Chacabuco 145, 4000 S.M. Tucumán, Argentina
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  • Graciela Font de Valdez,

    1. Centro de Referencia para Lactobacilos (CERELA, CONICET), Chacabuco 145, 4000 S.M. Tucumán, Argentina
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  • Åsa Ljungh

    1. Department of Medical Microbiology, Dermatology and Infection, University of Lund, Sölvegatan 23, S-223 62 Lund, Sweden
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*Corresponding author. Tel.: +54 (381) 4310465; Fax: +54 (381) 3311720, E-mail: glorca@cerela.org.ar

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.

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