NDLI: Temperature-Dependent Expression of Listeria monocytogenes Internalin and Internalin-Like Genes Suggests Functional Diversity of These Proteins among the Listeriae▿ †

Content Provider	PubMed Central
Author	Mcgann, Patrick Ivanek, Renata Wiedmann, Martin Boor, Kathryn J.
Copyright Year	2007
Abstract	The Listeria monocytogenes genome contains genes encoding several internalins and internalin-like proteins. As L. monocytogenes is present in many environments and can infect numerous, diverse host species, the environmental temperature was hypothesized to be a signal that might affect internalin gene transcription. A subgenomic microarray was used to investigate temperature-dependent transcription of 24 members of the internalin gene family in L. monocytogenes 10403S. The levels of internalin gene transcripts for cells grown at 37°C were compared to the levels of transcripts for cells grown at 16, 30, and 42°C using competitive microarray hybridization, and the results were confirmed by performing quantitative reverse transcriptase PCR for 14 internalin genes. Based on these studies, the internalin genes can be grouped into the following five temperature-dependent categories: (i) four σB-dependent internalin genes (inlC2, inlD, lmo0331, and lmo0610) with the highest levels of transcripts at 16°C and generally the lowest levels of transcripts at 37°C; (ii) three partially PrfA-dependent internalin genes (inlA, inlB, and inlC) with the lowest levels of transcripts at 16°C and the highest levels of transcripts at 37 and 42°C; (iii) four genes (inlG, inlJ, lmo0514, and lmo1290) with the lowest levels of transcripts at 16°C and the highest levels of transcripts at 30 and/or 37°C; (iv) one gene (lmo0327) with the highest levels of transcripts at 16°C and low levels of transcripts at higher temperatures; and (v) 12 internalin genes with no differences in the levels of transcripts at the temperatures used in this study. The temperature-dependent transcription patterns suggest that the relative importance of different internalins varies by environment, which may provide insight into the specific functions of these proteins.
Related Links	http://dx.doi.org/10.1128/AEM.02923-06
Starting Page	2806
File Format	PDF
ISSN	10985336
e-ISSN	10985336
Journal	Applied and Environmental Microbiology
Issue Number	9
Volume Number	73
Language	English
Publisher	American Society for Microbiology
Publisher Date	2007-05-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Ecology Food Science Applied Microbiology and Biotechnology Biotechnology

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