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Immunolocalization of the Novel Protein FCHSD2 within Protrusive Actin‐Rich Bacterial Structures
Author(s) -
Walker Brittany D.,
Almeida-Souza Leonardo,
Guttman Julian A.
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.02054
Subject(s) - microbiology and biotechnology , actin , endocytosis , biology , clathrin , actin cytoskeleton , actin binding protein , microfilament , actin remodeling , cytoskeleton , cell , biochemistry
Listeria monocytogenes and enteropathogenic E. coli (EPEC) both exploit clathrin mediated endocytosis and the actin cytoskeleton for their disease processes. During L. monocytogenes infections clathrin is used for the microbes to invade their host’s cells and actin filaments are used to generate actin‐rich comet/rocket tails that propel the bacteria within the host cell cytoplasm. When the bacteria hit the host plasma membrane, the comet/rocket tails push the bacteria into neighbouring cells by forming a membrane distention housing the bacteria and the actin tail which forms a corresponding invagination in the neighbouring cell for eventual cell‐to‐cell spreading of the bacteria. EPEC on the other hand remains extracellular and sit atop infected cells on actin‐rich pedestal‐like structures that also recruit clathrin to their apical regions. The FCH and double SH3 domains protein 2 (FCHSD2) functions to activate actin polymerization during clathrin mediated endocytosis. As both L. monocytogenes an EPEC utilize CME and actin polymerization we examined the localization of FCHSD2 during the infections. We found that during L. monocytogenes infections FCHSD2 was absent from the bacterial comet tails, but was prominent at L. monocytogenes actin‐rich membrane protrusions. During EPEC infections FCHSD2 was present within the actin core of the pedestals but did not colocalize with clathrin. Together, this work suggests the FCHSD2 protein has a distinct role at actin‐rich bacterial structures that interact at the membrane which is independent of clathrin.