Burkholderia pseudomallei type III secreted protein BipC: role in actin modulation and translocation activities required for the bacterial intracellular lifecycle

Melioidosis, an infection caused by the facultative intracellular pathogen , has been classified as an emerging disease with the number of patients steadily increasing at an alarming rate. possess various virulence determinants that allow them to invade the host and evade the host immune response, s...

Full description

Saved in:

Bibliographic Details
Published in:	PeerJ (San Francisco, CA) CA), 2016-12, Vol.4, p.e2532-e2532, Article e2532
Main Authors:	Kang, Wen Tyng, Vellasamy, Kumutha Malar, Rajamani, Lakshminarayanan, Beuerman, Roger W, Vadivelu, Jamuna
Format:	Article
Language:	eng
Subjects:	Actin Actin dynamics Bacteria Bioinformatics Burkholderia pseudomallei Cloning Depolymerization E coli Effector protein Escherichia coli Genetic engineering Health aspects Homology Immune response Infections Infectious Diseases Internalization Intracellular Intracellular lifecycle Lymphocytes B Melioidosis Microbiology Mortality Muscle proteins Pathogenesis Pathogens Plasmids Polymerization Protein expression and purification Proteins Shigella Type III secretion system Virulence
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	Melioidosis, an infection caused by the facultative intracellular pathogen , has been classified as an emerging disease with the number of patients steadily increasing at an alarming rate. possess various virulence determinants that allow them to invade the host and evade the host immune response, such as the type III secretion systems (TTSS). The products of this specialized secretion system are particularly important for the infection. Lacking in one or more components of the TTSS demonstrated different degrees of defects in the intracellular lifecycle of . Further understanding the functional roles of proteins involved in TTSS will enable us to dissect the enigma of -host cell interaction. In this study, BipC (a translocator), which was previously reported to be involved in the pathogenesis of , was further characterized using the bioinformatics and molecular approaches. The gene, coding for a putative invasive protein, was first PCR amplified from K96243 genomic DNA and cloned into an expression vector for overexpression in . The soluble protein was subsequently purified and assayed for actin polymerization and depolymerization. BipC was verified to subvert the host actin dynamics as demonstrated by the capability to polymerize actin . Homology modeling was also attempted to predict the structure of BipC. Overall, our findings identified that the protein encoded by the gene plays a role as an effector involved in the actin binding activity to facilitate internalization of into the host cells.
ISSN:	2167-8359 2167-8359