Glycosylation is a ubiquitous post-translational modification responsible for a multitude of
crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to …

Hemagglutinin (HA) is most abundant glycoprotein on the influenza virus surface. Influenza
HA promotes viral entry by engaging the receptor and mediating virus–host membrane …

Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best
available examples of the humoral immune response to HIV are providing important …

Seasonal influenza A viruses (IAV) originate from pandemic IAV and have undergone
changes in antigenic structure, including addition of glycans to the hemagglutinin (HA) …

Influenza virus evolves rapidly to constantly escape from natural immunity. Most humoral
immune responses to influenza virus target the hemagglutinin (HA) glycoprotein, which is …

Arenaviruses such as Lassa virus (LASV) can cause severe hemorrhagic fever in humans.
As a major impediment to vaccine development, delayed and weak neutralizing antibody …

To ensure that vaccination offers the best protection against an infectious disease, sequence
identity between the vaccine and the circulating strain is paramount. During replication of …

Influenza virus hemagglutinin consists of a highly variable and immunodominant head
domain and a more conserved but immunosubdominant stalk domain. We introduced seven …

Despite advancements in immunotherapeutic approaches, influenza continues to cause
severe illness, particularly among immunocompromised individuals, young children, and …

Hemagglutinin (HA) glycoprotein is an important focus of influenza research due to its role in
antigenic drift and shift, as well as its receptor binding and membrane fusion functions …