Abstract

Various bacterial pathogens display an intracellular lifestyle and spread from cell to cell through actin-based motility (ABM). ABM requires actin polymerization at the bacterial pole and is mediated by the expression of bacterial factors that hijack the host cell actin nucleation machinery or exhibit intrinsic actin nucleation properties. It is increasingly recognized that bacterial ABM factors, in addition to having a crucial task during the intracellular phase of infection, display "moonlighting" adhesin functions, such as bacterial aggregation, biofilm formation, and host cell adhesion/invasion. Here, we review our current knowledge of ABM factors and their additional functions, and we propose that intracellular ABM functions have evolved from ancestral, extracellular adhesin functions.

Highlights

  • Various bacterial pathogens display an intracellular lifestyle and spread from cell to cell through actin-based motility (ABM)

  • Extracellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) operates as a virulence factor, contributing to bacterial adherence to host cells [7,8,9], to interactions between different bacterial species that facilitate host colonization [10], and to evasion from the host immune system [7, 11, 12]

  • We discuss the extracellular moonlighting functions of bacterial factors that support the intracellular lifestyle of cytosolic pathogens displaying actin-based motility (ABM)

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Summary

Introduction

Various bacterial pathogens display an intracellular lifestyle and spread from cell to cell through actin-based motility (ABM). We discuss the extracellular moonlighting functions of bacterial factors that support the intracellular lifestyle of cytosolic pathogens displaying actin-based motility (ABM). Various intracellular pathogens, such as Listeria monocytogenes, Shigella flexneri, Rickettsia spp., and Burkholderia spp., reside in the cytosol of infected cells, where they acquire ABM through expression of bacterial factors that hijack the host cell actin polymerization machinery or exhibit intrinsic actin nucleation capacity [13].

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