hemagglutinin/dental caries

This study demonstrated that sublingual immunization with a fusion protein, 25k-hagA-MBP, which consists of a 25-kDa antigenic region of hemagglutinin A purified from Porphyromonas gingivalis fused to maltose-binding protein (MBP) originating from Escherichia coli as an adjuvant, elicited protective

Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry.

Cleavage of influenza A virus hemagglutinin (HA) is required for expression of fusion activity and virus entry into cells. Extracellular proteases are responsible for the proteolytic cleavage activation of avirulent avian and mammalian influenza viruses and contribute to pathogenicity and tissue

BACKGROUND Synthetic hemozoin (sHZ, also known as β-hematin) from monomeric heme is a particle adjuvant which activates antigen-presenting cells (APCs), such as dendritic cells and macrophages, and enhances humoral immune responses to several antigens, including ovalbumin, human serum albumin, and

We studied the influence of calcium on lipid mixing mediated by influenza hemagglutinin (HA). Lipid mixing between HA-expressing cells and liposomes containing disialoganglioside, influenza virus receptor, was studied at 37 degrees C and neutral pH after a low-pH pulse at 4 degrees C. With

For influenza virus hemagglutinin, an N-cap structure, created at low pH, interacts with membrane-proximal residues (173-178), bringing fusion peptides and membrane-spanning domains close together. Mutational analysis was used to define the role of these interactions in membrane fusion. For all

The human parainfluenza virus type 3 (hPIV3) hemagglutinin-neuraminidase (HN) has opposing functions of binding sialic acid receptors and cleaving them, facilitating virus release. The crystal structure of hPIV3 HN complexed with the substrate analogue difluorosialic acid (DFSA) revealed that

Influenza A viruses (IAV) have been a major public health threat worldwide, and options for antiviral therapy become increasingly limited with the emergence of drug-resisting virus strains. New and effective anti-IAV drugs, especially for highly pathogenic influenza, with different modes of action,

The influenza virus hemagglutinin is a potential drug target for antivirus treatment. A variety of membrane fusion inhibitors targeting hemagglutinin have been discovered, but the binding sites and modes, important for understanding membrane fusion and rational drug design, have not yet been

Hemagglutinins to xenogeneic erythrocytes were increased in rats if intraperitoneal immunization was performed during the healing phase of a chemical peritonitis. Increased absorption of the antigen into lymph nodes draining the peritoneal cavity was probably responsible for the enhanced immune

Nowadays, influenza virus is still a big threat to human. Hemagglutinin (HA) and neuraminidase (NA) are the two viral surface proteins, which play important roles in the life cycle of influenza virus. Current influenza vaccines and anti-influenza drugs work mainly by interfering with the functions

This study brings the analysis of amino acid sequences of hemagglutinin (HA) from the influenza virus A that can infect a wide variety of birds and mammals. 191 sequences belonging to all known 15 HA subtypes were compared. The emphasis was given on functional sites (receptor-binding cavity with its

Measles virus hemagglutinin (MVH) residues potentially responsible for attachment to the wild-type (wt) MV receptor SLAM (CD150) have been identified and localized on the MVH globular head by reference to a revised hypothetical structural model for MVH (www.pepscan.nl/downloads/measlesH.pdb). We