Huibin Lv

Jan 15, 2025 | cell.com | Qi Wen Teo |Yiquan Wang |Huibin Lv |Michael S. Oade |Kevin J. Mao |Timothy J.C. Tan | +8 more

Keywordsinfluenza virusNS1nuclear export proteinNEPevolutionary constraintsthe transcription-to-replication switchinnate immune responsecellular apoptosismammalian adaptation of avian influenza virusResearch topic(s)CP: MicrobiologyCP: Molecular biologyIntroductionInfluenza A virus (IAV) belongs to the Orthomyxoviridae family and is characterized as an enveloped, negative-sense, single-stranded, segmented RNA virus.

May 18, 2024 | biorxiv.org | Qi Wen Teo |Yiquan Wang |Huibin Lv |Kevin J. Mao

AbstractThe influenza A virus nuclear export protein (NEP) is a multifunctional protein that is essential for the viral life cycle and has very high sequence conservation. However, since the open reading frame of NEP largely overlaps with that of another influenza viral protein, non-structural protein 1, it is difficult to infer the functional constraints of NEP based on sequence conservation analysis.

Apr 22, 2024 | biorxiv.org | Huibin Lv |Qi Wen Teo |Chang-Chun D. Lee |Weiwen Liang

AbstractUnderstanding how immune history influences influenza immunity is essential for developing effective vaccines and therapeutic strategies. This study investigates the antigenic imprinting of influenza hemagglutinin (HA) and neuraminidase (NA) using a mouse model with sequential infection by four seasonal H1N1 strains.

Nov 15, 2023 | cell.com | Qi Wen Teo |Yiquan Wang |Huibin Lv |Timothy J.C. Tan

Highlights•Compatibilities of CR9114 with diverse light chains and CDR H3s are probed•Light chain of CR9114, despite having no contact with the epitope, is important for binding•Most CDR H3s from other IGHV1-69 HA stem antibodies are incompatible with CR9114SummaryIGHV1-69 is frequently utilized by broadly neutralizing influenza antibodies to the hemagglutinin (HA) stem. These IGHV1-69 HA stem antibodies have diverse complementarity-determining region (CDR) H3 sequences.

Sep 14, 2023 | biorxiv.org | Yiquan Wang |Huibin Lv |Ruipeng Lei |Yuen-Hei Yeung

AbstractDespite decades of antibody research, it remains challenging to predict the specificity of an antibody solely based on its sequence. Two major obstacles are the lack of appropriate models and inaccessibility of datasets for model training. In this study, we curated a dataset of >5,000 influenza hemagglutinin (HA) antibodies by mining research publications and patents, which revealed many distinct sequence features between antibodies to HA head and stem domains.