Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

Severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoVs) are zoonotic pathogens with high fatality rates and pandemic potential. Vaccine development focuses on the principal target of the neutralizing humoral immune response, the spike (S) glycoprotei...

Descrizione completa

Dettagli Bibliografici
Autori principali:	Watanabe, Y, Berndsen, ZT, Raghwani, J, Seabright, GE, Allen, JD, Pybus, OG, McLellan, JS, Wilson, IA, Bowden, TA, Ward, AB, Crispin, M
Natura:	Journal article
Lingua:	English
Pubblicazione:	Springer Nature 2020

Documenti analoghi

Vulnerabilities in coronavirus glycan shields despite extensive glycosylation
di: Yasunori Watanabe, et al.
Pubblicazione: (2020-05-01)

Structure of the Lassa virus glycan shield provides a model for immunological resistance
di: Watanabe, Y, et al.
Pubblicazione: (2018)

Antibodies expose multiple weaknesses in the glycan shield of HIV.
di: Crispin, M, et al.
Pubblicazione: (2013)

Antibodies expose multiple weaknesses in the glycan shield of HIV.
di: Crispin, M, et al.
Pubblicazione: (2013)

The impact of sequence diversity on the glycan shield of HIV-1 immunogens
di: Seabright, GE
Pubblicazione: (2019)

Beyond Shielding: The Roles of Glycans in the SARS-CoV‑2 Spike Protein
di: Lorenzo Casalino, et al.
Pubblicazione: (2020-09-01)

Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies.
di: Pritchard, L, et al.
Pubblicazione: (2015)

Architecture of the HIV-1 glycan shield
di: Pritchard, L
Pubblicazione: (2014)

Mapping the glycan shields of enveloped viruses
di: Watanabe, Y
Pubblicazione: (2020)

Integrity of glycosylation processing of a glycan-depleted trimeric HIV-1 immunogen targeting key B-cell lineages
di: Behrens, AJ, et al.
Pubblicazione: (2018)

The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
di: Joel D. Allen, et al.
Pubblicazione: (2023-04-01)

The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade.
di: Bonomelli, C, et al.
Pubblicazione: (2011)

Glycosylator: a Python framework for the rapid modeling of glycans
di: Thomas Lemmin, et al.
Pubblicazione: (2019-10-01)

N- and O-glycan analysis for the detection of glycosylation disorders
di: Amr Sobhi Gouda, et al.
Pubblicazione: (2021-01-01)

Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies
di: Le, N, et al.
Pubblicazione: (2016)

The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade.
di: Camille Bonomelli, et al.
Pubblicazione: (2011-01-01)

Fine structure of the HIV-1 glycan shield
di: Behrens, A
Pubblicazione: (2017)

Glycan shield of the ebolavirus envelope glycoprotein GP
di: Weiwei Peng, et al.
Pubblicazione: (2022-08-01)

Conformational Heterogeneity of the HIV Envelope Glycan Shield
di: Mingjun Yang, et al.
Pubblicazione: (2017-06-01)

Glycan Nanostructures of Human Coronaviruses
di: Guo W, et al.
Pubblicazione: (2021-07-01)

Arenavirus glycan shield promotes neutralizing antibody evasion and protracted infection.
di: Sommerstein, R, et al.
Pubblicazione: (2015)

Arenavirus Glycan Shield Promotes Neutralizing Antibody Evasion and Protracted Infection.
di: Rami Sommerstein, et al.
Pubblicazione: (2015-11-01)

Synthesis of N-glycan oxazolines: donors for endohexosaminidase catalysed glycosylation.
di: Rising, T, et al.
Pubblicazione: (2006)

Editorial: Glycobiology and glycosylation: deciphering the secrets of glycans in humans and pathogens
di: Parham Jabbarzadeh Kaboli, et al.
Pubblicazione: (2025-02-01)

N-Glycosylation and N-Glycan Processing in HBV Biology and Pathogenesis
di: Mihaela-Olivia Dobrica, et al.
Pubblicazione: (2020-06-01)

Glycosylation network mapping and site-specific glycan maturation in vivo
di: Marie-Estelle Losfeld, et al.
Pubblicazione: (2022-11-01)

Recognition and penetration of the HIV-1 Env glycan shield by potent broadly neutralizing antibodies
di: Julien J, et al.
Pubblicazione: (2012-09-01)

Glycan Positioning Impacts HIV-1 Env Glycan-Shield Density, Function, and Recognition by Antibodies
di: Qing Wei, et al.
Pubblicazione: (2020-11-01)

Antibody evasion by a gammaherpesvirus O-glycan shield.
di: Bénédicte Machiels, et al.
Pubblicazione: (2011-11-01)

Glycan Profile Analysis of Engineered Trastuzumab with Rationally Added Glycosylation Sequons Presents Significantly Increased Glycan Complexity
di: Esteban Cruz, et al.
Pubblicazione: (2021-10-01)

Emerging COVID-19 coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26
di: Naveen Vankadari, et al.
Pubblicazione: (2020-01-01)

A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield
di: Pejchal, R, et al.
Pubblicazione: (2011)

Glycans instructing immunity: the emerging role of altered glycosylation in clinical immunology
di: Jonathan J Lyons, et al.
Pubblicazione: (2015-06-01)

Multivalent interactions between fully glycosylated influenza virus hemagglutinins mediated by glycans at distinct N-glycosylation sites
di: Ruofan Li, et al.
Pubblicazione: (2024-10-01)

Fine structure of the HIV-1 glycan shield - Supplementary information
di: Behrens, A
Pubblicazione: (2017)

Quantification of the Impact of the HIV-1-Glycan Shield on Antibody Elicitation
di: Tongqing Zhou, et al.
Pubblicazione: (2017-04-01)

Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies
di: Muriel Lavie, et al.
Pubblicazione: (2018-04-01)

Structural constraints determine the glycosylation of HIV-1 envelope trimers
di: Pritchard, L, et al.
Pubblicazione: (2015)

Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.
di: Rajesh P Ringe, et al.
Pubblicazione: (2023-10-01)

Controlled site-selective protein glycosylation for precise glycan structure-catalytic activity relationships.
di: Davis, B, et al.
Pubblicazione: (2000)