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Crystallization and preliminary x-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei

Crystallization and preliminary x-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei
Crystallization and preliminary x-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei
Burkholderia pseudomallei, the causative agent of melioidosis, possesses a protein-secretion apparatus that is similar to those found in Salmonella and Shigella. A major function of these secretion systems is to secrete virulence-associated proteins into target cells of the host organism. The BipD gene of B. pseudomallei encodes a secreted virulence factor that is similar in sequence and most likely functionally analogous to IpaD from Shigella and SipD from Salmonella. Thus, the BipD protein is likely to be a component of a type III protein-secretion system (TTSS) in B. pseudomallei. Proteins in the same class as BipD, such as IpaD and SipD, are thought to act as extracellular chaperones to help the hydrophobic translocator proteins enter the target cell membrane, where they form a pore and might even link the translocon pore with the secretion needle. There is evidence that the translocator proteins also bind an integrin which stimulates actin-mediated insertion of the bacterium into the host-cell membrane. Native BipD has been crystallized in a monoclinic crystal form that diffracts X-rays to 2.5 Å resolution. BipD protein which incorporates selenomethionine (SeMet-BipD) has also been expressed and forms crystals which diffract to a higher resolution of 2.1 Å.
2053-230X
761-764
Knight, M.J.
3f836d6c-f83f-41bd-a2f4-4da770ac1e8d
Ruaux, A.
e079ff49-40e7-4866-8f4c-8087e1224db5
Mikolajek, H.
c394c255-9248-4217-ace9-4a0382bfc0c5
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Gill, R.
95656ecb-604f-425e-ac66-7dd36e47d94d
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Wood, M.
e80db4b2-cf82-4044-a37c-2e23c031e14e
Cooper, J. B.
123b9e61-1a61-4802-a764-6452c238f4ab
Knight, M.J.
3f836d6c-f83f-41bd-a2f4-4da770ac1e8d
Ruaux, A.
e079ff49-40e7-4866-8f4c-8087e1224db5
Mikolajek, H.
c394c255-9248-4217-ace9-4a0382bfc0c5
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Gill, R.
95656ecb-604f-425e-ac66-7dd36e47d94d
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Wood, M.
e80db4b2-cf82-4044-a37c-2e23c031e14e
Cooper, J. B.
123b9e61-1a61-4802-a764-6452c238f4ab

Knight, M.J., Ruaux, A., Mikolajek, H., Erskine, P.T., Gill, R., Wood, S.P., Wood, M. and Cooper, J. B. (2006) Crystallization and preliminary x-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei. Acta Crystallographica Section F: Structural Biology Communications, 62, part 8, 761-764. (doi:10.1107/S1744309106024857). (PMID:16880550)

Record type: Article

Abstract

Burkholderia pseudomallei, the causative agent of melioidosis, possesses a protein-secretion apparatus that is similar to those found in Salmonella and Shigella. A major function of these secretion systems is to secrete virulence-associated proteins into target cells of the host organism. The BipD gene of B. pseudomallei encodes a secreted virulence factor that is similar in sequence and most likely functionally analogous to IpaD from Shigella and SipD from Salmonella. Thus, the BipD protein is likely to be a component of a type III protein-secretion system (TTSS) in B. pseudomallei. Proteins in the same class as BipD, such as IpaD and SipD, are thought to act as extracellular chaperones to help the hydrophobic translocator proteins enter the target cell membrane, where they form a pore and might even link the translocon pore with the secretion needle. There is evidence that the translocator proteins also bind an integrin which stimulates actin-mediated insertion of the bacterium into the host-cell membrane. Native BipD has been crystallized in a monoclinic crystal form that diffracts X-rays to 2.5 Å resolution. BipD protein which incorporates selenomethionine (SeMet-BipD) has also been expressed and forms crystals which diffract to a higher resolution of 2.1 Å.

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Published date: August 2006
Organisations: Centre for Biological Sciences

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Local EPrints ID: 337112
URI: http://eprints.soton.ac.uk/id/eprint/337112
ISSN: 2053-230X
PURE UUID: 9e4c161f-599b-4128-92f8-6cd1f0786647
ORCID for H. Mikolajek: ORCID iD orcid.org/0000-0003-0776-9974

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Date deposited: 18 Apr 2012 11:05
Last modified: 14 Mar 2024 10:49

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Contributors

Author: M.J. Knight
Author: A. Ruaux
Author: H. Mikolajek ORCID iD
Author: P.T. Erskine
Author: R. Gill
Author: S.P. Wood
Author: M. Wood
Author: J. B. Cooper

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