Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment

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dc.contributor.author Jones, Robert T.
dc.contributor.author Sanchez-Contreras, Maria
dc.contributor.author Vlisidou, Isabella
dc.contributor.author Amos, Matthew R.
dc.contributor.author Yang, Guowei
dc.contributor.author Muñoz-Berbel, Xavier
dc.contributor.author Upadhyay, Abhishek
dc.contributor.author Potter, Ursula J.
dc.contributor.author Joyce, Susan A.
dc.contributor.author Ciche, Todd A.
dc.contributor.author Jenkins, A. Toby A.
dc.contributor.author Bagby, Stefan
dc.contributor.author ffrench-Constant, Richard H.
dc.contributor.author Waterfield, Nicholas R.
dc.date.accessioned 2018-02-07T09:48:36Z
dc.date.available 2018-02-07T09:48:36Z
dc.date.issued 2010-05-12
dc.identifier.citation Jones, R. T., Sanchez-Contreras, M., Vlisidou, I., Amos, M. R., Yang, G., Muñoz-Berbel, X., Upadhyay, A., Potter, U. J., Joyce, S. A., Ciche, T. A., Jenkins, A. T. A., Bagby, S., ffrench-Constant, R. H. and Waterfield, N. R. (2010) 'Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment', BMC Microbiology, 10(1), 141 (13 pp). doi: 10.1186/1471-2180-10-141 en
dc.identifier.volume 10 en
dc.identifier.issued 1 en
dc.identifier.startpage 141 en
dc.identifier.issn 1471-2180
dc.identifier.uri http://hdl.handle.net/10468/5416
dc.identifier.doi 10.1186/1471-2180-10-141
dc.description.abstract Background: Photorhabdus are Gram-negative nematode-symbiotic and insect-pathogenic bacteria. The species Photorhabdus asymbiotica is able to infect humans as well as insects. We investigated the secreted proteome of a clinical isolate of P. asymbiotica at different temperatures in order to identify proteins relevant to the infection of the two different hosts. Results: A comparison of the proteins secreted by a clinical isolate of P. asymbiotica at simulated insect (28°C) and human (37°C) temperatures led to the identification of a small and highly abundant protein, designated Pam, that is only secreted at the lower temperature. The pam gene is present in all Photorhabdus strains tested and shows a high level of conservation across the whole genus, suggesting it is both ancestral to the genus and probably important to the biology of the bacterium. The Pam protein shows limited sequence similarity to the 13.6 kDa component of a binary toxin of Bacillus thuringiensis. Nevertheless, injection or feeding of heterologously produced Pam showed no insecticidal activity to either Galleria mellonella or Manduca sexta larvae. In bacterial colonies, Pam is associated with an extracellular polysaccharide (EPS)-like matrix, and modifies the ability of wild-type cells to attach to an artificial surface. Interestingly, Surface Plasmon Resonance (SPR) binding studies revealed that the Pam protein itself has adhesive properties. Although Pam is produced throughout insect infection, genetic knockout does not affect either insect virulence or the ability of P. luminescens to form a symbiotic association with its host nematode, Heterorhabditis bacteriophora. Conclusions: We studied a highly abundant protein, Pam, which is secreted in a temperature-dependent manner in P. asymbiotica. Our findings indicate that Pam plays an important role in enhancing surface attachment in insect blood. Its association with exopolysaccharide suggests it may exert its effect through mediation of EPS properties. Despite its abundance and conservation in the genus, we find no evidence for a role of Pam in either virulence or symbiosis. en
dc.description.sponsorship Wellcome Trust (grant 076124) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher BioMed Central en
dc.rights © 2010 Jones et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. en
dc.subject Photorhabdus en
dc.subject Photorhabdus asymbiotica en
dc.subject Infection en
dc.subject Insect blood en
dc.title Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Susan Joyce, School Of Biochemistry & Cell Biology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: s.joyce@ucc.ie en
dc.internal.availability Full text available en
dc.date.updated 2018-02-07T09:33:31Z
dc.description.version Published Version en
dc.internal.rssid 424843626
dc.contributor.funder Biotechnology and Biological Sciences Research Council en
dc.contributor.funder Wellcome Trust en
dc.contributor.funder Seventh Framework Programme en
dc.description.status Peer reviewed en
dc.identifier.journaltitle BMC Microbiology en
dc.internal.copyrightchecked No !!CORA!! en
dc.internal.licenseacceptance Yes en
dc.internal.IRISemailaddress s.joyce@ucc.ie en
dc.relation.project info:eu-repo/grantAgreement/RCUK/BBSRC/BB/E021328/1/GB/Rapid bacterial Virulence Annotation for the post genomic era/ en
dc.relation.project info:eu-repo/grantAgreement/EC/FP7::SP1::NMP/211436/EU/Development and analysis of polymer based multi-functional bactericidal materials/EMBEK1 en


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