A Framework for Interpreting the Leucine-Rich Repeats of the Listeria Internalins

The surface protein InlB of the bacterial pathogen Listeria monocytogenes is required for inducing phagocytosis in various nonphagocytic mammalian cell types in vitro. InlB causes tyrosine phosphorylation of host cell adaptor proteins, activation of phosphoinositide 3-kinase, and rearrangements of t...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 97; no. 16; pp. 8784 - 8788
Main Authors Marino, Michael, Braun, Laurence, Cossart, Pascale, Ghosh, Partho
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 01.08.2000
National Acad Sciences
National Academy of Sciences
The National Academy of Sciences
SeriesColloquium Paper
Subjects
Amino Acid Sequence
Bacteria
Bacterial Proteins - chemistry
Cell lines
Cells
Chemistry
Epithelial cells
Hepatocytes
Hydrogen
inlA protein
inlB protein
internalin
Leucine - chemistry
Listeria
Listeria - chemistry
Listeria internalins
Molecular Sequence Data
Molecules
Papers from the National Academy of Sciences Colloquium on Virulence and Defense in Host-Pathogen Interactions: Common Features between Plants and Animals
Pathogens
Phagocytes
Phagocytosis
phosphoinositide 3-kinase
Proteins
Sequence Homology, Amino Acid
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Summary:The surface protein InlB of the bacterial pathogen Listeria monocytogenes is required for inducing phagocytosis in various nonphagocytic mammalian cell types in vitro. InlB causes tyrosine phosphorylation of host cell adaptor proteins, activation of phosphoinositide 3-kinase, and rearrangements of the actin cytoskeleton. These events lead to phagocytic uptake of the bacterium by the host cell. InlB belongs to the internalin family of Listeria proteins, which also includes InlA, another surface protein involved in host cell invasion. The internalins are the largest class of bacterial proteins containing leucine-rich repeats (LRR), a motif associated with protein-protein interactions. The LRR motif is found in a functionally diverse array of proteins, including those involved in the plant immune system and in the mammalian innate immune response. Structural and functional interpretations of the sequences of internalin family members are presented in light of the recently determined x-ray crystal structure of the InlB LRR domain.
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To whom reprint requests should be addressed. E-mail: pghosh@ucsd.edu.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.97.16.8784