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

Michael Marino, Laurence Braun, Pascale Cossart and Partho Ghosh
Proceedings of the National Academy of Sciences of the United States of America
Vol. 97, No. 16 (Aug. 1, 2000), pp. 8784-8788
Stable URL: http://www.jstor.org/stable/123082
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
A Framework for Interpreting the Leucine-Rich Repeats of the Listeria Internalins
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Abstract

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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