Ehrlichia chaffeensis TRP32 interacts with host cell targets that influence intracellular survival

Tian Luo, Jere McBride

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Ehrlichia chaffeensis is an obligately intracellular bacterium that exhibits tropism for mononuclear phagocytes and survives by evading host cell defense mechanisms. Recently, molecular interactions of E. chaffeensis tandem repeat proteins 47 and 120 (TRP47 and -120) and the eukaryotic host cell have been described. In this investigation, yeast two-hybrid analysis demonstrated that an E. chaffeensis type 1 secretion system substrate, TRP32, interacts with a diverse group of human proteins associated with major biological processes of the host cell, including protein synthesis, trafficking, degradation, immune signaling, cell signaling, iron metabolism, and apoptosis. Eight target proteins, including translation elongation factor 1 alpha 1 (EF1A1), deleted in azoospermia (DAZ)-associated protein 2 (DAZAP2), ferritin light polypeptide (FTL), CD63, CD14, proteasome subunit beta type 1 (PSMB1), ring finger and CCCH-type domain 1 (RC3H1), and tumor protein p53-inducible protein 11 (TP53I11) interacted with TRP32 as determined by coimmunoprecipitation assays, colocalization with TRP32 in HeLa and THP-1 cells, and/or RNA interference. Interactions between TRP32 and host targets localized to the E. chaffeensis morulae or in the host cell cytoplasm adjacent to morulae. Common or closely related interacting partners of E. chaffeensis TRP32, TRP47, and TRP120 demonstrate a molecular convergence on common cellular processes and molecular cross talk between Ehrlichia TRPs and host targets. These findings further support the role of TRPs as effectors that promote intracellular survival.

Original languageEnglish (US)
Pages (from-to)2297-2306
Number of pages10
JournalInfection and Immunity
Volume80
Issue number7
DOIs
StatePublished - Jul 2012

Fingerprint

Ehrlichia chaffeensis
Survival
Morula
Translational Peptide Chain Elongation
Proteins
Ehrlichia
Peptide Elongation Factor 1
Biological Phenomena
Tandem Repeat Sequences
Tropism
Eukaryotic Cells
Protein Transport
Proteasome Endopeptidase Complex
Phagocytes
Ferritins
RNA Interference
Fingers
Cytoplasm
Iron
Yeasts

ASJC Scopus subject areas

  • Immunology
  • Microbiology
  • Parasitology
  • Infectious Diseases

Cite this

Ehrlichia chaffeensis TRP32 interacts with host cell targets that influence intracellular survival. / Luo, Tian; McBride, Jere.

In: Infection and Immunity, Vol. 80, No. 7, 07.2012, p. 2297-2306.

Research output: Contribution to journalArticle

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