The Hendra virus vaccine: perceptions regarding the role of antibody titre testing

Author(s):  
RS Barrett ◽  
A Wiethoelter ◽  
K Halpin

2008 ◽  
Vol 15 (7) ◽  
pp. 1042-1053 ◽  
Author(s):  
Bruce D. Forrest ◽  
Michael W. Pride ◽  
Andrew J. Dunning ◽  
Maria Rosario Z. Capeding ◽  
Tawee Chotpitayasunondh ◽  
...  

ABSTRACT The highly sensitive gamma interferon (IFN-γ) enzyme-linked immunosorbent spot (ELISPOT) assay permits the investigation of the role of cell-mediated immunity (CMI) in the protection of young children against influenza. Preliminary studies of young children confirmed that the IFN-γ ELISPOT assay was a more sensitive measure of influenza memory immune responses than serum antibody and that among seronegative children aged 6 to <36 months, an intranasal dose of 107 fluorescent focus units (FFU) of a live attenuated influenza virus vaccine (CAIV-T) elicited substantial CMI responses. A commercial inactivated influenza virus vaccine elicited CMI responses only in children with some previous exposure to related influenza viruses as determined by detectable antibody levels prevaccination. The role of CMI in actual protection against community-acquired, culture-confirmed clinical influenza by CAIV-T was investigated in a large randomized, double-blind, placebo-controlled dose-ranging efficacy trial with 2,172 children aged 6 to <36 months in the Philippines and Thailand. The estimated protection curve indicated that the majority of infants and young children with ≥100 spot-forming cells/106 peripheral blood mononuclear cells were protected against clinical influenza, establishing a possible target level of CMI for future influenza vaccine development. The ELISPOT assay for IFN-γ is a sensitive and reproducible measure of CMI and memory immune responses and contributes to establishing requirements for the future development of vaccines against influenza, especially those used for children.



2013 ◽  
Vol 91 (8) ◽  
pp. 328-331 ◽  
Author(s):  
D Mendez ◽  
P Büttner ◽  
R Speare
Keyword(s):  




PLoS ONE ◽  
2013 ◽  
Vol 8 (5) ◽  
pp. e63163 ◽  
Author(s):  
Natalija Budimir ◽  
Aalzen de Haan ◽  
Tjarko Meijerhof ◽  
Simke Waijer ◽  
Louis Boon ◽  
...  


2005 ◽  
Vol 79 (12) ◽  
pp. 7922-7925 ◽  
Author(s):  
James Richard Carter ◽  
Cara Theresia Pager ◽  
Stephen Derrick Fowler ◽  
Rebecca Ellis Dutch

ABSTRACT The Hendra virus fusion (F) protein contains five potential sites for N-linked glycosylation in the ectodomain. Examination of F protein mutants with single asparagine-to-alanine mutations indicated that two sites in the F2 subunit (N67 and N99) and two sites in the F1 subunit (N414 and N464) normally undergo N-linked glycosylation. While N-linked modification at N414 is critical for protein folding and transport, F proteins lacking carbohydrates at N67, N99, or N464 remained fusogenically active. As N464 lies within heptad repeat B, these results contrast with those seen for several paramyxovirus F proteins.



2017 ◽  
Vol 13 (1) ◽  
Author(s):  
J. Manyweathers ◽  
H. Field ◽  
N. Longnecker ◽  
K. Agho ◽  
C. Smith ◽  
...  


2012 ◽  
Vol 86 (6) ◽  
pp. 3003-3013 ◽  
Author(s):  
E. C. Smith ◽  
M. R. Culler ◽  
L. M. Hellman ◽  
M. G. Fried ◽  
T. P. Creamer ◽  
...  




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