ArticleBMC microbiology2010
Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment.
Article in BMC microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Advanced Genetic and Molecular Techniques for Improving Biocontrol Traits of Entomopathogenic Nematodes.International journal of molecular sciences · 2026Review
- Organic Acid Exposure Enhances Virulence in SomeFrontiers in microbiology · 2021Article
- Temperature Restriction in Entomopathogenic Bacteria.Frontiers in microbiology · 2020Article
- Dialkylresorcinols as bacterial signaling molecules.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- From Insect to Man: Photorhabdus Sheds Light on the Emergence of Human Pathogenicity.PloS one · 2015Article
- Structural and biophysical characterization of Bacillus thuringiensis insecticidal proteins Cry34Ab1 and Cry35Ab1.PloS one · 2014Article
- The insect Galleria mellonella as a powerful infection model to investigate bacterial pathogenesis.Journal of visualized experiments : JoVE · 2012Article
- Influence of the Photorhabdus luminescens phosphomannose isomerase gene, manA, on mannose utilization, exopolysaccharide structure, and biofilm formation.Applied and environmental microbiology · 2011Article
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
Abstract
backgroundPhotorhabdus 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.
resultsA comparison of the proteins secreted by a clinical isolate of P. asymbiotica at simulated insect (28 degrees C) and human (37 degrees 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.
conclusionsWe 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.
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