Link to the University of Pittsburgh Homepage
Link to the University Library System Homepage Link to the Contact Us Form

A Potential Role for the Interaction of Wolbachia Surface Proteins with the Brugia malayi Glycolytic Enzymes and Cytoskeleton in Maintenance of Endosymbiosis

Melnikow, E and Xu, S and Liu, J and Bell, AJ and Ghedin, E and Unnasch, TR and Lustigman, S (2013) A Potential Role for the Interaction of Wolbachia Surface Proteins with the Brugia malayi Glycolytic Enzymes and Cytoskeleton in Maintenance of Endosymbiosis. PLoS Neglected Tropical Diseases, 7 (4). ISSN 1935-2727

[img]
Preview
PDF
Published Version
Available under License : See the attached license file.

Download (1MB) | Preview
[img] Plain Text (licence)
Available under License : See the attached license file.

Download (1kB)

Abstract

The human filarial parasite Brugia malayi harbors an endosymbiotic bacterium of the genus Wolbachia. The Wolbachia represent an attractive target for the control of filarial induced disease as elimination of the bacteria affects molting, reproduction and survival of the worms. The molecular basis for the symbiotic relationship between Wolbachia and their filarial hosts has yet to be elucidated. To identify proteins involved in this process, we focused on the Wolbachia surface proteins (WSPs), which are known to be involved in bacteria-host interactions in other bacterial systems. Two WSP-like proteins (wBm0152 and wBm0432) were localized to various host tissues of the B. malayi female adult worms and are present in the excretory/secretory products of the worms. We provide evidence that both of these proteins bind specifically to B. malayi crude protein extracts and to individual filarial proteins to create functional complexes. The wBm0432 interacts with several key enzymes involved in the host glycolytic pathway, including aldolase and enolase. The wBm0152 interacts with the host cytoskeletal proteins actin and tubulin. We also show these interactions in vitro and have verified that wBm0432 and B. malayi aldolase, as well as wBm0152 and B. malayi actin, co-localize to the vacuole surrounding Wolbachia. We propose that both WSP protein complexes interact with each other via the aldolase-actin link and/or via the possible interaction between the host's enolase and the cytoskeleton, and play a role in Wolbachia distribution during worm growth and embryogenesis. © 2013 Melnikow et al.


Share

Citation/Export:
Social Networking:
Share |

Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Melnikow, E
Xu, S
Liu, J
Bell, AJ
Ghedin, Eelg21@pitt.eduELG21
Unnasch, TR
Lustigman, S
Centers: Other Centers, Institutes, or Units > Center for Vaccine Research
Date: 1 January 2013
Date Type: Publication
Journal or Publication Title: PLoS Neglected Tropical Diseases
Volume: 7
Number: 4
DOI or Unique Handle: 10.1371/journal.pntd.0002151
Schools and Programs: School of Medicine > Computational and Systems Biology
Refereed: Yes
ISSN: 1935-2727
Date Deposited: 03 May 2013 21:00
Last Modified: 29 Jan 2019 15:55
URI: http://d-scholarship.pitt.edu/id/eprint/18325

Metrics

Monthly Views for the past 3 years

Plum Analytics

Altmetric.com


Actions (login required)

View Item View Item