期刊
ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY
卷 95, 期 4, 页码 363-372出版社
SPRINGER
DOI: 10.1007/s10482-009-9322-y
关键词
Glycosylation; Immunochemistry; Lactobacillus kefir; S-layer; Spectrometry
类别
资金
- Agencia Nacional de Investigaciones Cientificas y Tecnologicas (ANPCyT)
- Consejo Nacional de Investigaciones Cientificas y Tecnologicas (CONICET)
- Comision de Investigaciones Cientificas de la Provincia de Buenos Aires (CIC PBA)
- Facultad de Ciencias Exactas, Universidad Nacional de La Plata (UNLP)
- Genoma Spain
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.
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