Hormogonia are the infective agents in many cyanobacterium-plant symbioses. Pilus-like appendages are expressed on the hormogonium surface, and mutations in pil-like genes altered surface piliation and reduced symbiotic competency. This is the first molecular evidence that pilus biogenesis in a filamentous cyanobacterium requires a type IV pilus system.
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http://dx.doi.org/10.1128/JB.01927-06 | DOI Listing |
J Biol Chem
November 2024
Institute for Molecular Biosciences, Goethe-University Frankfurt/M., Frankfurt, Germany; Center for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt/M., Frankfurt, Germany. Electronic address:
c-di-GMP is an important second messenger in bacteria regulating, for example motility, biofilm formation, cell wall biosynthesis, infectivity, and natural transformability. It binds to a multitude of intracellular receptors. This includes proteins containing general secretory pathway II (GSPII) domains such as the N-terminal domain of the Vibrio cholerae ATPase MshE (MshEN) which binds c-di-GMP with two copies of a 24-amino acids sequence motif.
View Article and Find Full Text PDFFront Microbiol
September 2024
Enteric Diseases Laboratory Branch, Centers for Disease Control and Prevention, Atlanta, GA, United States.
is an emerging foodborne pathogen. We previously reported that some avian Shiga toxin-producing strains exhibited higher or comparable cytotoxicity in Vero-d2EGFP cells with several enterohemorrhagic (EHEC) outbreak strains. To better understand the environmental persistence of this pathogen, comparative genomics and phenotypic assays were applied to assess adhesion capability, motility, and biofilm formation in .
View Article and Find Full Text PDFProc Natl Acad Sci U S A
October 2024
Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO 63110.
Gram-negative bacteria produce chaperone-usher pathway pili, which are extracellular protein fibers tipped with an adhesive protein that binds to a receptor with stereochemical specificity to determine host and tissue tropism. The outer-membrane usher protein, together with a periplasmic chaperone, assembles thousands of pilin subunits into a highly ordered pilus fiber. The tip adhesin in complex with its cognate chaperone activates the usher to allow extrusion across the outer membrane.
View Article and Find Full Text PDFAnnu Rev Microbiol
November 2024
Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, California, USA.
Arch Microbiol
August 2024
Departamento de Microbiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad 2001, Col. Chamilpa, Cuernavaca, Mor, 62210, Mexico.
Adherence to both cellular and abiotic surfaces is a crucial step in the interaction of bacterial pathogens and commensals with their hosts. Bacterial surface structures known as fimbriae or pili play a fundamental role in the early colonization stages by providing specificity or tropism. Among the various fimbrial families, the chaperone-usher family has been extensively studied due to its ubiquity, diversity, and abundance.
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