The composition of the Gram-positive cell wall is typically described as containing
peptidoglycan, proteins and essential secondary cell wall structures called teichoic acids …

Protein glycosylation, the attachment of sugars to amino acid side chains, can endow
proteins with a wide variety of properties of great interest to the engineering biology …

Summary Asparagine (N) 297-linked glycosylation of immunoglobulin G (IgG) Fc is required
for binding to FcγRIIa, IIb, and IIIa, although it is unclear how it contributes. We found the …

Glycans or carbohydrates attached to therapeutic glycoproteins can directly affect product
quality, safety and efficacy, and therefore must be adequately analyzed and controlled …

The increasing demand for recombinant vaccine antigens or immunotherapeutic molecules
calls into question the universality of current protein expression systems. Vaccine production …

Colanic acid (CA) is a natural polysaccharide macromolecule with rich and unique
biological properties and is a promising candidate for use in food and cosmetics. To date …

Urinary tract infection (UTI) is a major infectious disease commonly induced by
uropathogenic Escherichia coli (UPEC), of which a prevalent serogroup is the mostly …

The central enzyme in the Campylobacter jejuni asparagine-linked glycosylation pathway is
the oligosaccharyltransferase (OST), PglB, which transfers preassembled glycans to specific …

The recent advancement in the human glycome and progress in the development of an
inclusive network of glycosylation pathways allow the incorporation of suitable machinery for …

Site selectivity of protein N-linked glycosylation is dependent on many factors, including
accessibility of the modification site, amino acid composition of the glycosylation consensus …