Interplay of virulence factors and signaling molecules: albumin and calcium-mediated biofilm regulation in Bordetella bronchiseptica [PDF]
Bordetella bronchiseptica, a respiratory pathogen capable of infecting various mammals, including humans, is associated with chronic infections. B.
Sabrina Laura Mugni +4 more
doaj +4 more sources
Pathogenicity and virulence of Bordetella pertussis and its adaptation to its strictly human host
The highly contagious whooping cough agent Bordetella pertussis has evolved as a human-restricted pathogen from a progenitor which also gave rise to Bordetella parapertussis and Bordetella bronchiseptica.
Camille Locht +2 more
exaly +2 more sources
The Type III Secreted Protein BspR Regulates the Virulence Genes in Bordetella bronchiseptica [PDF]
Bordetella bronchiseptica is closely related with B. pertussis and B. parapertussis, the causative agents of whooping cough. These pathogenic species share a number of virulence genes, including the gene locus for the type III secretion system (T3SS ...
Asaomi Kuwae, Akio Abe, Jun Kurushima
exaly +2 more sources
Bordetella bronchiseptica is a leading cause of respiratory diseases in pigs. However, epidemiological data of B. bronchiseptica in pigs particularly in China, the largest pig rearing country in the world is still limited.
Zhong Peng, Yue Zhang, Bin Wu
exaly +3 more sources
Bordetella BcrH1 and BcrH2 Are Specific Chaperones for the Pore-Forming Complex. [PDF]
ABSTRACT Bordetella has a type III secretion system that secretes virulence proteins crucial to the establishment of infection. The genes encoding components of the Bordetella type III secretion system are located in the bsc region on the chromosome. This region includes the bcrH1 and bcrH2 genes, which respectively encode the proteins BcrH1 and BcrH2.
Kishino Y +4 more
europepmc +2 more sources
A Case of Sepsis Caused by ST80 Multidrug-Resistant Enterococcus faecium With Concurrent Klebsiella pneumoniae Infection in a Dog. [PDF]
An 8‐year‐old dog developed acute respiratory distress that progressed to sepsis and death. Multidrug‐resistant Enterococcus faecium ST80 was isolated from the liver and kidney, while Klebsiella pneumoniae was detected in the lung by PCR. Whole‐genome sequencing showed that the ST80 isolates were genetically identical, suggesting hematogenous spread ...
Seo HM +5 more
europepmc +2 more sources
Released palmitic acid–mediated TLR4/NF-κB activation enhances the virulence of Bordetella pertussis MT28 lineage [PDF]
Whooping cough has resurged globally despite high vaccination coverage. In China, a macrolide-resistant (MR) Bordetella pertussis lineage carrying the high-virulence ptxP3 allele, termed ptxP3 MR-MT28 (MT28), has been increasingly reported as a ...
Shuangshuang Li +17 more
doaj +2 more sources
From Lake Victoria to the Tap: Antibiotic Resistance and Pathogenic Contamination of Kisumu City Water Supply and Wastewater Network. [PDF]
ABSTRACT Waterborne diseases and antimicrobial resistance (AMR) pose mounting public health threats across sub‐Saharan Africa, particularly in rapidly urbanising regions dependent on untreated or poorly treated surface waters. This study applied shotgun metagenomic sequencing to characterise microbial communities, virulence factors and antibiotic ...
Reva ON +8 more
europepmc +2 more sources
Nuanced differences in adenylate cyclase toxin production, acylation, and secretion may contribute to the evolution of virulence in Bordetella species [PDF]
Bordetella pertussis, which causes the acute human disease whooping cough, evolved from Bordetella bronchiseptica, which causes long-term, chronic infections in a broad range of mammals. Both B. pertussis and B.
Alexa R. Wolber +5 more
doaj +2 more sources
Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding. [PDF]
Abstract Disulphide bonds (Dsbs) are essential for the folding, stability, and function of many secreted and membrane‐associated proteins in bacteria. In Gram‐negative species, these bonds are introduced by the Dsb enzyme family, with DsbA acting as the primary thiol oxidase.
Penning S +9 more
europepmc +2 more sources

