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Viruses 2018, 10(8), 426; https://doi.org/10.3390/v10080426

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

1
Laboratory of Microbiology, Parasitology and Hygiene, University of Antwerp, B-2610 Antwerp, Belgium
2
Laboratory of Cell Biology and Histology, University of Antwerp, B-2610 Antwerp, Belgium
3
Medical Biotechnology Centre, VIB, B-9052 Ghent, Belgium
4
Department of Biomedical Molecular Biology, Ghent University, B-9052 Ghent, Belgium
5
The Pirbright Institute, Surrey GU24 0NF, UK
6
Laboratory of Physiopharmacology, University of Antwerp, B-2610 Antwerp, Belgium
*
Author to whom correspondence should be addressed.
Received: 23 July 2018 / Revised: 8 August 2018 / Accepted: 13 August 2018 / Published: 14 August 2018
(This article belongs to the Section Antivirals & Vaccines)
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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. View Full-Text
Keywords: class I fusion protein; virus glycosylation; DNA immunization; humoral responses; pneumovirus; vaccine class I fusion protein; virus glycosylation; DNA immunization; humoral responses; pneumovirus; vaccine
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Leemans, A.; Boeren, M.; Van der Gucht, W.; Pintelon, I.; Roose, K.; Schepens, B.; Saelens, X.; Bailey, D.; Martinet, W.; Caljon, G.; Maes, L.; Cos, P.; Delputte, P. 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. Viruses 2018, 10, 426.

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