English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

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.

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