Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains

Pablo Mobili, María de los Ángeles Serradell, Sebastián A. Trejo, Francesc X. Avilés Puigvert, Analía G. Abraham, Graciela L. De Antoni

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44 Citations (Scopus)

Abstract

Since the presence of S-layer protein conditioned the autoaggregation capacity of some strains of Lactobacillus kefir, S-layer proteins from aggregating and non-aggregating L. kefir strains were characterized by immunochemical reactivity, MALDI-TOF spectrometry and glycosylation analysis. Two anti-S-layer monoclonal antibodies (Mab5F8 and Mab1F8) were produced; in an indirect enzyme-linked immunosorbent assay Mab1F8 recognized S-layer proteins from all L. kefir tested while Mab5F8 recognized only S-layer proteins from aggregating strains. Periodic Acid-Schiff staining of proteins after polyacrylamide gel electrophoresis under denaturing conditions revealed that all L. kefir S-layer proteins tested were glycosylated. Growth of bacteria in the presence of the N-glycosylation inhibitor tunicamycin suggested the presence of glycosydic chains O-linked to the protein backbone. MALDI-TOF peptide map fingerprint for S-layer proteins from 12 L. kefir strains showed very similar patterns for the aggregating strains, different from those for the non-aggregating ones. No positive match with other protein spectra in MSDB Database was found. Our results revealed a high heterogeneity among S-layer proteins from different L. kefir strains but also suggested a correlation between the structure of these S-layer glycoproteins and the aggregation properties of whole bacterial cells. © Springer Science+Business Media B.V. 2009.
Original languageEnglish
Pages (from-to)363-372
JournalAntonie van Leeuwenhoek, International Journal of General and Molecular Microbiology
Volume95
Issue number4
DOIs
Publication statusPublished - 8 Apr 2009

Keywords

  • Glycosylation
  • Immunochemistry
  • Lactobacillus kefir
  • S-layer
  • Spectrometry

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