Immunodominant Domains Present on theBordetella pertussisVaccine Component Filamentous Hemagglutinin [PDF]
To identify immunologically important domains on filamentous hemagglutinin (FHA), a Bordetella pertussis protein included in new acellular pertussis vaccines (ACPVs), a series of monoclonal antibodies, sera from infants vaccinated with ACPVs or whole cell pertussis vaccine (WCPV), and sera from patients with pertussis were analyzed by immunoblots ...
E, Leininger +7 more
openaire +2 more sources
Forward Genetic Dissection of Biofilm Development by Fusobacterium nucleatum: Novel Functions of Cell Division Proteins FtsX and EnvC. [PDF]
Fusobacterium nucleatum is a key member of the human oral biofilm. It is also implicated in preterm birth and colorectal cancer. To facilitate basic studies of fusobacterial virulence, we describe here a versatile transposon mutagenesis procedure and a ...
Abu Amar Mohamed Al Mamun +10 more
core +2 more sources
Influenza A virus surface proteins are organized to help penetrate host mucus
Influenza A virus (IAV) enters cells by binding to sialic acid on the cell surface. To accomplish this while avoiding immobilization by sialic acid in host mucus, viruses rely on a balance between the receptor-binding protein hemagglutinin (HA) and the ...
Michael D Vahey, Daniel A Fletcher
doaj +1 more source
Viral factors in influenza pandemic risk assessment [PDF]
The threat of an influenza A virus pandemic stems from continual virus spillovers from reservoir species, a tiny fraction of which spark sustained transmission in humans.
Barclay, Wendy +18 more
core +4 more sources
Long-lived respiratory immune response to filamentous hemagglutinin following Bordetella pertussis infection [PDF]
Systemic and mucosal B-cell-mediated immune responses to purified filamentous hemagglutinin (FHA) in mice were analyzed at different times following a single respiratory infection with Bordetella pertussis. Serum immunoglobulin G (IgG) anti-FHA and respiratory IgG and IgA anti-FHA antibodies were first detected at 3 weeks postinfection, reached high ...
D F, Amsbaugh, Z M, Li, R D, Shahin
openaire +2 more sources
Cryotomography of budding influenza a virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end [PDF]
Influenza viruses exhibit striking variations in particle morphology between strains. Clinical isolates of influenza A virus have been shown to produce long filamentous particles while laboratory-adapted strains are predominantly spherical.
A Ali +45 more
core +3 more sources
Inhibition ofBordetella pertussisfilamentous hemagglutinin-mediated cell adherence with monoclonal antibodies [PDF]
Filamentous hemagglutinin (FHA), a 220-kDa protein located on the surface of Bordetella pertussis, is one of the major cell adhesins of this bacterium. We have produced three hybridoma cell lines that express monoclonal antibodies (mAbs) against FHA: X3C, X3E and X4B.
E, Leininger +3 more
openaire +3 more sources
New Data on Vaccine Antigen Deficient Bordetella pertussis Isolates
Evolution of Bordetella pertussis is driven by natural and vaccine pressures. Isolates circulating in regions with high vaccination coverage present multiple allelic and antigenic variations as compared to isolates collected before introduction of ...
Valérie Bouchez +4 more
doaj +1 more source
1705. Filamentous Hemagglutinin Polyclonal Antibodies Protect against Multidrug resistant Gram-negative bacteria [PDF]
Abstract Background Multidrug-resistant (MDR) Gram-negative bacteria (GNB) are among the major healthcare-associated infections and have high mortality especially in immunocompromised patients. Acinetobacter baumannii (AB) and Pseudomonas aeruginosa (PA) are classified as “critical organism” by CDC ...
Youssef, Eman +4 more
europepmc +2 more sources
Bordetella pertussis binds the human complement regulator C4BP: role of filamentous hemagglutinin [PDF]
C4BP (C4b-binding protein) is a high-molecular-weight plasma protein that inhibits the classical pathway of complement activation. Recent experiments have demonstrated that C4BP binds to many strains of the gram-positive bacterium Streptococcus pyogenes, a major respiratory tract pathogen. Binding to S.
Berggard, K +3 more
openaire +3 more sources

