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Showing 1–4 of 4 results

Advanced filters: Author: Tala Azzam Clear advanced filters

Asymmetrically glycosylated IgG1 antibodies are universal and drive human disease

Authors show that all individuals have asymmetrically glycosylated IgGs—the glycans on each of the Fc protomers are not identical. Asymmetrically monofucosylated IgGs drive dengue disease and are functionally similar to afucosylated IgGs.

Tala Azzam
Stylianos Bournazos
Eric J. Sundberg
ResearchOpen Access12 Dec 2025
Nature Communications

Volume: 17, P: 1-16
The mechanistic basis for interprotomer deglycosylation of antibodies by corynebacterial IgG-specific endoglycosidases

Here the authors define an inter-protomeric mechanism of deglycosylation of human IgG antibodies for corynebacterial IgG-specific ENGases and demonstrate that in vivo CU43 treatment preserve the neutralizing capacity of anti-influenza IgG antibodies.

Diego E. Sastre
Stylianos Bournazos
Eric J. Sundberg
ResearchOpen Access04 Jul 2025
Nature Communications

Volume: 16, P: 1-17
Novel HIV-1 fusion peptide immunogens using glycan-engineered alphavirus-like particles

Seo-Ho Oh
Dedeepya R. Gudipati
Rui Kong
ResearchOpen Access14 Nov 2025
npj Vaccines

Volume: 10, P: 1-14
Global estimates on the number of people blind or visually impaired by Uncorrected Refractive Error: a meta-analysis from 2000 to 2020

Julie-Anne Little
Nathan G. Congdon
Rupert Bourne
ResearchOpen Access04 Jul 2024
Eye

Volume: 38, P: 2083-2101