Attachment Strength of Listeria monocytogenes and its Internalin-Negative Mutants |
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| Authors: | B Y Chen T J Kim Y S Jung J L Silva |
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| Institution: | (1) Department of Food Science, Nutrition, and Health Promotion, Mississippi State University, Box 9805, Starkville, MS, USA;(2) Department of Biochemistry and Molecular Biology, Mississippi State University, Starkville, MS 39762, USA |
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| Abstract: | A single cell of Listeria monocytogenes attached on food contact surfaces can be a potential source of cross-contamination in a food-processing plant. To see whether
internalin A (InlA) and B (InlB), major surface proteins on L. monocytogenes, play a significant role in the attachment process, wild-type L. monocytogenes EGD (LM_EGD) and its isogenic internalin-negative mutants (LM_EGDΔinlA, LM_EGDΔinlB, and LM_EGDΔinlAB) were used to determine attachment strength on inert glass surface. Western blot analysis using InlA and InlB antibodies
confirmed the absence of InlA in LM_EGDΔinlA, InlB in LM_EGDΔinlB, and both InlA and InlB in LM_EGDΔinlAB. Regardless of initial attachment numbers, LM_EGD which expressed both InlA and InlB proteins exhibited the strongest attachment
strength while the double mutant (LM_EGDΔinlAB) exhibited the weakest. The two single mutants (LM_EGDΔinlA and LM_EGDΔinlB) that expressed only one type of the internalins were shown to have intermediate attachment strength. These results suggest
that both InlA and InlB expression play a significant role in the attachment strength of L. monocytogenes on glass surface. |
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| Keywords: | Listeria monocytogenes Isogenic internalin-negative mutants InlA InlB Attachment strength Western blot analysis |
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