Publication
Title
Removal of the N-glycosylation sequon at position N116 located in p27 of the respiratory syncytial virus fusion protein elicits enhanced antibody responses after DNA immunization
Author
Abstract
Prevention of severe lower respiratory tract infections in infants caused by the human respiratory syncytial virus (hRSV) remains a major public health priority. Currently, the major focus of vaccine development relies on the RSV fusion (F) protein since it is the main target protein for neutralizing antibodies induced by natural infection. The protein conserves 5 N-glycosylation sites, two of which are located in the F2 subunit (N27 and N70), one in the F1 subunit (N500) and two in the p27 peptide (N116 and N126). To study the influence of the loss of one or more N-glycosylation sites on RSV F immunogenicity, BALB/c mice were immunized with plasmids encoding RSV F glycomutants. In comparison with F WT DNA immunized mice, higher neutralizing titres were observed following immunization with F N116Q. Moreover, RSV A2-K-line19F challenge of mice that had been immunized with mutant F N116Q DNA was associated with lower RSV RNA levels compared with those in challenged WT F DNA immunized animals. Since p27 is assumed to be post-translationally released after cleavage and thus not present on the mature RSV F protein, it remains to be elucidated how deletion of this glycan can contribute to enhanced antibody responses and protection upon challenge. These findings provide new insights to improve the immunogenicity of RSV F in potential vaccine candidates.
Language
English
Source (journal)
Viruses
Viruses
Publication
2018
ISSN
1999-4915
Volume/pages
10 :8 (2018) , 20 p.
Article Reference
426
ISI
000443619600037
Pubmed ID
30110893
Medium
E-only publicatie
Full text (Publisher's DOI)
Full text (open access)
UAntwerpen
Faculty/Department
Research group
Project info
Characterisation of a novel Respiratory Syncytial Virus (RSV) immune evasion mechanism and evaluation of the impact for development of novel vaccines and prophylactic and/or therapeutic antibodies
Improved respiratory syncytial virus (rsv) vaccines based on glycan modification of the viral fusion (f) protein.
Mechanism of infection of sialoadhesin (Sn)-positive macrophages with respiratory syncytial virus (RSV) and its implications for inflammation and immune pathology during bronchiolitis.
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 06.09.2018
Last edited 19.10.2021
To cite this reference