Affiliation:
1. Department of Life Sciences1 and
2. Department of Plant and Soil Science,2 Alabama A&M University, Normal, Alabama 35762, and
3. Department of Food Science, Purdue University, West Lafayette, Indiana 479073
Abstract
ABSTRACT
Interaction of
Listeria monocytogenes
with mammalian intestinal cells is believed to be an important first step in
Listeria
pathogenesis. Transposon (Tn
916
) mutagenesis provided strong evidence that a 104-kDa surface protein, designated the
Listeria
adhesion protein (LAP), was involved in adherence of
L. monocytogenes
to a human enterocyte-like Caco-2 cell line (V. Pandiripally, D. Westbrook, G. Sunki, and A. Bhunia, J. Med. Microbiol. 48:117–124, 1999). In this study, expression of LAP in
L. monocytogenes
at various growth temperatures (25, 37, and 42°C) and in various growth phases was determined by performing an enzyme-linked immunoassay (ELISA) and Western blotting with a specific monoclonal antibody (monoclonal antibody H7). The ELISA and Western blot results indicated that there was a significant increase in LAP expression over time only at 37 and 42°C and that the level of LAP expression was low during the exponential phase and high during the stationary phase. In contrast, there were not significant differences in LAP expression between the exponential and stationary phases at 25°C. Examination of the adhesion of
L. monocytogenes
cells from exponential-phase (12-h) or stationary-phase (24-h) cultures grown at 37°C to Caco-2 cells revealed that there were not significant differences in adhesion. Although expression of
L. monocytogenes
LAP was different at different growth temperatures and in different growth phases, enhanced expression did not result in increased adhesion, possibly because only a few LAP molecules were sufficient to initiate binding to Caco-2 cells.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
32 articles.
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