Abstract：
:Development of recombinant protective antigen (rPA)-based anthrax vaccines has been hindered by a lack of stability of the vaccines associated with spontaneous deamidation of asparagine (Asn) residues of the rPA antigen during storage. In this study, we explored the role that two deamidation-prone Asn residues located directly adjacent to the receptor binding site of PA, Asn713 and Asn719, play in the stability of rPA-based anthrax vaccines. We modified these residues to glutamine (Gln) and generated rPA(N713Q/N719Q), since Gln would not be expected to deamidate on a time scale relevant to vaccine storage. While wild-type rPA vaccine formulated with aluminum hydroxide lost immunogenicity upon storage, as measured by induction of toxin-neutralizing antibodies in mice, the rPA(N713Q/N719Q) vaccine did not exhibit a significant loss in immunogenicity. This finding suggests that modification of Asn713 and Asn719 of rPA to deamidation-resistant amino acids may improve the stability of rPA-based anthrax vaccines.
journal_name
Vaccinejournal_title
Vaccineauthors
Verma A,Burns DLdoi
10.1016/j.vaccine.2018.09.012subject
Has Abstractpub_date
2018-10-15 00:00:00pages
6379-6382issue
43eissn
0264-410Xissn
1873-2518pii
S0264-410X(18)31261-1journal_volume
36pub_type
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