The bacterium Pseudoalteromonas tunicata is a common surface colonizer of marine eukaryotes, including the macroalga Ulva australis.Genomic analysis of P. tunicata identified genes potentially involved in surface colonization, including genes with homology to bacterial virulence factors that mediate attachment. Of particular interest is the presence of a gene, designated ptlL32, encoding an ortholog to the Leptospira lipoprotein LipL32, which has been shown to facilitate the interaction of Leptospira sp. with host extracellular matrix (ECM) structures and is thought to be an important virulence trait for pathogenic Leptospira. To investigate the role of PtlL32 in the colonization by P. tunicata we constructed and characterized a ΔptlL32 mutant strain. Whilst P. tunicata ΔptlL32 bound to an abiotic surface with the same capacity as the wild type strain, it had a marked effect on the ability of P. tunicata to bind to ECM, suggesting a specific role in attachment to biological surfaces. Loss of PtlL32 also significantly reduced the capacity for P. tunciata to colonize the host algal surface demonstrating a clear role for this protein as a host-colonization factor. PtlL32 appears to have a patchy distribution across specific groups of environmental bacteria and phylogenetic analysis of PtlL32 orthologous proteins from non-Leptospira species suggests it may have been acquired via horizontal gene transfer between distantly related lineages. This study provides the first evidence for an attachment function for a LipL32-like protein outside the Leptospira and thereby contributes to the understanding of host colonization in ecologically distinct bacterial species.
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http://dx.doi.org/10.3389/fmicb.2014.00323 | DOI Listing |
bioRxiv
September 2024
Section of Infectious Disease, Department of Internal Medicine, School of Medicine, Yale University, New Haven, CT.
Biometals
December 2024
Department of Microbiology, Immunology and Parasitology, Federal University of Santa Catarina (UFSC), Av. Delfino Conti, S/N-Trindade, Florianópolis, SC, 88040-900, Brazil.
Leptospires, as motile Gram-negative bacteria, employ sophisticated strategies for efficient invasion and dissemination within their hosts. In response, hosts counteract pathogens through nutritional immunity, a concept involving the deprivation of essential metals such as zinc. Zinc, pivotal in modulating pathogen-host interactions, influences proteins structural, catalytic, and regulatory functions.
View Article and Find Full Text PDFSci Rep
August 2024
Department of Medicine, University of Connecticut Health, 263 Farmington Avenue, Farmington, CT, 06030-3715, USA.
The Omp85 family of outer membrane proteins are ubiquitously distributed among diderm bacteria and play essential roles in outer membrane (OM) biogenesis. The majority of Omp85 orthologs are bipartite and consist of a conserved OM-embedded 16-stranded beta-barrel and variable periplasmic functional domains. Here, we demonstrate that Leptospira interrogans encodes four distinct Omp85 proteins.
View Article and Find Full Text PDFMicroorganisms
January 2024
Department of Infection Biology and Microbiomes, Institute of Infection, Veterinary & Ecological Sciences, University of Liverpool, Leahurst Campus, Chester High Road, Neston CH64 7TE, UK.
Leptospirosis is a zoonotic bacterial disease affecting mammalian species worldwide. Cattle are a major susceptible host; infection with pathogenic spp. represents a public health risk and results in reproductive failure and reduced milk yield, causing economic losses.
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