Recombinant nanoparticle rsv f vaccine for respiratory syncytial virus
OwnerGale SMITH, Yingyun WU +2inventors
InventorsGale SMITH, Yingyun WU, Michael MASSARE, Ye LIU
Life of this patent
Estimating the term…
Abstract
The present invention is generally related to modified or mutated respiratory syncytial virus fusion (F) proteins and methods for making and using them, including immunogenic compositions such as vaccines for the treatment and/or prevention of RSV infection.
Claims21
1-76. (canceled)
A method of vaccinating a human against a viral infection comprising administering an RSV F vaccine to a human subject to obtain an immune response, wherein the RSV F vaccine comprises:
- (a) an RSV F protein trimer, wherein each RSV F protein of the trimer comprises
- (i) a deletion of one or more amino acids of the fusion domain, wherein said fusion domain corresponds to amino acids 137-146 of the wild-type RSV F protein (SEQ ID NO:
- 2), and
- (ii) an inactivated primary furin cleavage site, wherein the primary furin cleavage site corresponds to amino acids 131-136 of the wild-type RSV F protein (SEQ ID NO:
- 2), wherein the primary furin cleavage site is inactivated by amino acid substitution;
- (b) a pharmaceutically acceptable carrier, and
- (c) an alum adjuvant;
- wherein the immune response comprises antibodies that bind to a palivizumab epitope peptide on the RSV-F protein and wherein the antibodies are produced at a concentration of at least 40 μg/ml by 30 days after administration.
A method of inducing antibodies that bind to a palivizumab epitope peptide on the RSV-F protein in a human, comprising administering to the human intramuscularly an RSV F vaccine, comprising
- (a) an RSV F protein trimer, wherein each RSV F protein of the trimer comprises
- (i) a deletion of one or more amino acids of the fusion domain, wherein said fusion domain corresponds to amino acids 137-146 of the wild-type RSV F protein (SEQ ID NO:
- 2), and
- (ii) an inactivated primary furin cleavage site, wherein the primary furin cleavage site corresponds to amino acids 131-136 of the wild-type RSV F protein (SEQ ID NO:
- 2), wherein the primary furin cleavage site is inactivated by amino acid substitution;
- (b) a pharmaceutically acceptable carrier;
- and
- (c) an alum adjuvant;
- wherein the antibodies are produced at a concentration of at least 40 μg/ml by 30 days after administration.
Dependencies are inferred from the claim text.