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

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dc.contributor.authorJones, Robert T.
dc.contributor.authorSanchez-Contreras, Maria
dc.contributor.authorVlisidou, Isabella
dc.contributor.authorAmos, Matthew R.
dc.contributor.authorYang, Guowei
dc.contributor.authorMuñoz-Berbel, Xavier
dc.contributor.authorUpadhyay, Abhishek
dc.contributor.authorPotter, Ursula J.
dc.contributor.authorJoyce, Susan A.
dc.contributor.authorCiche, Todd A.
dc.contributor.authorJenkins, A. Toby A.
dc.contributor.authorBagby, Stefan
dc.contributor.authorffrench-Constant, Richard H.
dc.contributor.authorWaterfield, Nicholas R.
dc.contributor.funderBiotechnology and Biological Sciences Research Councilen
dc.contributor.funderWellcome Trusten
dc.contributor.funderSeventh Framework Programmeen
dc.date.accessioned2018-02-07T09:48:36Z
dc.date.available2018-02-07T09:48:36Z
dc.date.issued2010-05-12
dc.date.updated2018-02-07T09:33:31Z
dc.description.abstractBackground: 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.sponsorshipWellcome Trust (grant 076124)en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationJones, 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: 10.1186/1471-2180-10-141en
dc.identifier.doi10.1186/1471-2180-10-141
dc.identifier.issn1471-2180
dc.identifier.issued1en
dc.identifier.journaltitleBMC Microbiologyen
dc.identifier.startpage141en
dc.identifier.urihttps://hdl.handle.net/10468/5416
dc.identifier.volume10en
dc.language.isoenen
dc.publisherBioMed Centralen
dc.relation.projectinfo:eu-repo/grantAgreement/RCUK/BBSRC/BB/E021328/1/GB/Rapid bacterial Virulence Annotation for the post genomic era/en
dc.relation.projectinfo:eu-repo/grantAgreement/EC/FP7::SP1::NMP/211436/EU/Development and analysis of polymer based multi-functional bactericidal materials/EMBEK1en
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.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectPhotorhabdusen
dc.subjectPhotorhabdus asymbioticaen
dc.subjectInfectionen
dc.subjectInsect blooden
dc.titlePhotorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachmenten
dc.typeArticle (peer-reviewed)en
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