Bordetella pertussis and Bordetella bronchiseptica filamentous hemagglutinins are processed at different sites [PDF]
FEBS Open Bio, 2018 Filamentous hemagglutinin (FHA) mediates adherence and plays an important role in lower respiratory tract infections by pathogenic Bordetellae. The mature FHA proteins of B. pertussis (Bp‐FHA) and the B.
David Jurnecka +3 more
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Screening and Genomic Characterization of Filamentous Hemagglutinin-Deficient Bordetella pertussis. [PDF]
Infect Immun, 2018 ABSTRACT Despite high vaccine coverage, pertussis cases in the United States have increased over the last decade. Growing evidence suggests that disease resurgence results, in part, from genetic divergence of circulating strain populations away from vaccine references. The United States employs acellular vaccines exclusively, and
Weigand MR +16 more
europepmc +4 more sources
Filamentous Hemagglutinin of Bordetella pertussis Does Not Interact with the β2 Integrin CD11b/CD18. [PDF]
Int J Mol Sci, 2022 The pertussis agent Bordetella pertussis produces a number of virulence factors, of which the filamentous hemagglutinin (FhaB) plays a role in B. pertussis adhesion to epithelial and phagocytic cells. Moreover, FhaB was recently found to play a crucial role in nasal cavity infection and B. pertussis transmission to new hosts.
Golshani M +7 more
europepmc +4 more sources
Bordetella filamentous hemagglutinin and fimbriae: critical adhesins with unrealized vaccine potential. [PDF]
Pathog Dis, 2015 Pertussis, or whooping cough, is a highly contagious respiratory disease that is caused by the Gram-negative bacterium Bordetella pertussis, which is transmitted exclusively from human to human. While vaccination against B. pertussis has been successful, replacement of the whole cell vaccine with an acellular component vaccine has correlated with ...
Scheller EV, Cotter PA.
europepmc +4 more sources
<i>Bordetella</i> Filamentous Hemagglutinin, a Model for the Two-Partner Secretion Pathway. [PDF]
Microbiol Spectr, 2019 ABSTRACTBacteria use a variety of mechanisms to translocate proteins from the cytoplasm, where they are synthesized, to the cell surface or extracellular environment or directly into other cells, where they perform their ultimate functions. Type V secretion systems (T5SS) use β-barrel transporter domains to export passenger domains across the outer ...
Nash ZM, Cotter PA.
europepmc +4 more sources
Fha Deficient Bordetella pertussis Isolates in Iran with 50 Years Whole Cell Pertussis Vaccination
Iranian Journal of Public Health, 2021 Background: Bordetella pertussis, a highly contagious respiratory. Notably, the resurgence of pertussis has recently been associated with the lacking production of vaccine virulence factors.
Samaneh Saedi +5 more
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Interaction of theBordetella pertussisfilamentous hemagglutinin with heparin [PDF]
FEMS Microbiology Letters, 1991 Heparin, a glycosaminoglycan synthesized in connective tissue-mast cells, appeared to inhibit the hemagglutination of rabbit erythrocytes induced by the filamentous hemagglutinin (FHA), a major adhesin of Bordetella pertussis. This inhibition suggested an interaction of heparin with the FHA region responsible for the hemagglutination activity.
F D, Menozzi, C, Gantiez, C, Locht
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Antigenic Analysis of Bordetella pertussis Filamentous Hemagglutinin with Phage Display Libraries and Rabbit Anti-Filamentous Hemagglutinin Polyclonal Antibodies [PDF]
Infection and Immunity, 1998 ABSTRACT Although substantial advancements have been made in the development of efficacious acellular vaccines against Bordetella pertussis , continued progress requires better understanding of the antigenic makeup of B.
D R, Wilson, A, Siebers, B B, Finlay
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Vaccines, 2021 Pertussis is an acute respiratory tract infection caused by Bordetella pertussis. Even though its current vaccine coverage is relatively broad, they still have some shortcomings such as short protection time and might be incapable of blocking the spread ...
Han Xu +10 more
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Haemophilus ducreyi Secretes a Filamentous Hemagglutinin-Like Protein [PDF]
Journal of Bacteriology, 1998 ABSTRACT We have identified two extremely large open reading frames (ORFs) in Haemophilus ducreyi 35000, lspA1 and lspA2 , each of which encodes a predicted protein product whose N-terminal half is approximately 43% similar to the N-terminal half of
C K, Ward +4 more
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