H3N2 Canine
Sf9, Baculovirus cells.
Hemagglutinin
Description
Canine H3N2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 336 amino acids (18-344a.a.) and having a molecular mass of 36.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
H3N2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Hemagglutinin
Sf9, Baculovirus cells.
ADPNLPGNEN NAATLCLGHH AVPNGTIVKT ITDDQIEVTN ATELVQNSST GKICNNPHKI LDGRDCTLID ALLGDPHCDV FQNETWDLFV ERSNAFSNCY PYDVPDYASL RSIVASSGTL EFITEGFTWA GVTQNGGSGA CKRGPANGFF SRLNWLTKSG NTYPVLNVTM PNNNNFDKLY IWGVHHPSTN QEQTSLYIQA SGRVTVSTRR SQQTIIPNIG SRPLVRGQSG RISVYWTIVK PGDVLVINSN GNLIAPRGYF KMRIGKSSIM RSDAPIDTCI SECITPNGSI PNEKPFQNVN KITYGACPKY VKQNTLKLAT GMRNVPEKQT HHHHHH.
Product Science Overview
Hemagglutinin (HA) is a surface glycoprotein found on the Influenza A virus, playing a crucial role in the virus’s ability to infect host cells. The H3N2 subtype of Influenza A virus has been a significant concern due to its ability to infect various species, including humans, birds, and dogs. The canine recombinant form of H3N2 has garnered attention due to its implications for both veterinary and public health.
The H3N2 canine influenza virus (CIV) was first identified in 2006 in Guangdong, China. It is genetically closest to the H3N2 avian influenza virus (AIV) circulating in aquatic ducks in South Korea . Over the years, the virus has undergone several genetic changes, leading to the establishment of a stable virus lineage in dogs. Phylogenetic analysis has revealed multiple genotypes among H3N2 CIVs, with genotype 15 prevailing among dogs since around 2017 .
The hemagglutinin protein of H3N2 CIV has undergone various mutations that have facilitated its adaptation to mammalian hosts. Notable mutations include HA-G146S, HA-N188D, and HA-V223I . The V223I substitution, in particular, has been shown to reduce the virus’s binding affinity to human-type receptors while enhancing its thermal stability . This mutation is predominantly found in human and swine H3N2 viruses, suggesting its role in mammalian adaptation.
H3N2 CIVs have demonstrated the ability to bind both avian and human-type receptors. This dual receptor-binding capability is significant as it indicates the potential for cross-species transmission. Studies have shown that H3N2 CIVs can bind to human tracheal tissues, albeit with reduced affinity when carrying the HA-V223I mutation . This highlights the ongoing risk of zoonotic transmission and the necessity for close surveillance.
The emergence of H3N2 CIVs poses a potential threat to public health due to the close relationship between humans and dogs. Current human H3N2 vaccines do not confer protection against H3N2 CIVs, underscoring the need for the development of new vaccines and therapeutic strategies . The genetic variability and adaptability of H3N2 CIVs necessitate continuous monitoring to prevent potential outbreaks.
