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  1. Artikel: Stringent and complex sequence constraints of an IGHV1-69 broadly neutralizing antibody to influenza HA stem.

    Teo, Qi Wen / Wang, Yiquan / Lv, Huibin / Tan, Timothy J C / Lei, Ruipeng / Mao, Kevin J / Wu, Nicholas C

    bioRxiv : the preprint server for biology

    2023  

    Abstract: IGHV1-69 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. Besides, their light chains have minimal to ...

    Abstract IGHV1-69 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. Besides, their light chains have minimal to no contact with the epitope. Consequently, sequence determinants that confer IGHV1-69 antibodies with HA stem specificity remain largely elusive. Using high-throughput experiments, this study revealed the importance of light chain sequence for the IGHV1-69 HA stem antibody CR9114, which is the broadest influenza antibody known to date. Moreover, we demonstrated that the CDR H3 sequences from many other IGHV1-69 antibodies, including those to HA stem, were incompatible with CR9114. Along with mutagenesis and structural analysis, our results indicate that light chain and CDR H3 sequences coordinately determine the HA stem specificity of IGHV1-69 antibodies. Overall, this work provides molecular insights into broadly neutralizing antibody responses to influenza virus, which have important implications for universal influenza vaccine development.
    Sprache Englisch
    Erscheinungsdatum 2023-07-06
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.07.06.547908
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Stringent and complex sequence constraints of an IGHV1-69 broadly neutralizing antibody to influenza HA stem.

    Teo, Qi Wen / Wang, Yiquan / Lv, Huibin / Tan, Timothy J C / Lei, Ruipeng / Mao, Kevin J / Wu, Nicholas C

    Cell reports

    2023  Band 42, Heft 11, Seite(n) 113410

    Abstract: IGHV1-69 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. Besides, their light chains have minimal to ...

    Abstract IGHV1-69 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. Besides, their light chains have minimal to no contact with the epitope. Consequently, sequence determinants that confer IGHV1-69 antibodies with HA stem specificity remain largely elusive. Using high-throughput experiments, this study reveals the importance of light-chain sequence for the IGHV1-69 HA stem antibody CR9114, which is the broadest influenza antibody known to date. Moreover, we demonstrate that the CDR H3 sequences from many other IGHV1-69 antibodies, including those to the HA stem, are incompatible with CR9114. Along with mutagenesis and structural analysis, our results indicate that light-chain and CDR H3 sequences coordinately determine the HA stem specificity of IGHV1-69 antibodies. Overall, this work provides molecular insights into broadly neutralizing antibody responses to influenza virus, which have important implications for universal influenza vaccine development.
    Mesh-Begriff(e) Humans ; Influenza, Human ; Influenza Vaccines ; Hemagglutinins ; Broadly Neutralizing Antibodies ; Antibodies, Neutralizing ; Hemagglutinin Glycoproteins, Influenza Virus ; Antibodies, Viral ; Complementarity Determining Regions
    Chemische Substanzen Influenza Vaccines ; Hemagglutinins ; Broadly Neutralizing Antibodies ; Antibodies, Neutralizing ; Hemagglutinin Glycoproteins, Influenza Virus ; Antibodies, Viral ; Complementarity Determining Regions
    Sprache Englisch
    Erscheinungsdatum 2023-11-16
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2023.113410
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel: Deep mutational scanning of influenza A virus NEP reveals pleiotropic mutations in its N-terminal domain.

    Teo, Qi Wen / Wang, Yiquan / Lv, Huibin / Mao, Kevin J / Tan, Timothy J C / Huan, Yang Wei / Rivera-Cardona, Joel / Shao, Evan K / Choi, Danbi / Dargani, Zahra Tavakoli / Brooke, Christopher B / Wu, Nicholas C

    bioRxiv : the preprint server for biology

    2024  

    Abstract: The 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 ... ...

    Abstract The 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. Besides, the N-terminal of NEP is structurally disordered, which further complicates the understanding of its function. Here, we systematically measured the replication fitness effects of >1,800 mutations of NEP. Our results show that the N-terminal domain has high mutational tolerance. Additional experiments demonstrate that N-terminal domain mutations pleiotropically affect viral transcription and replication dynamics, host cellular responses, and mammalian adaptation of avian influenza virus. Overall, our study not only advances the functional understanding of NEP, but also provides insights into its evolutionary constraints.
    Sprache Englisch
    Erscheinungsdatum 2024-05-18
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2024.05.16.594574
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Thyroid arsenic content and papillary thyroid carcinoma arising 10 years after oral arsenic trioxide therapy for refractory acute promyelocytic leukemia.

    Au, Wing-yan / Lang, Brian H / Fong, Bonnie M W / Mao, Kevin J / Tam, Sidney

    Leukemia & lymphoma

    2013  Band 55, Heft 5, Seite(n) 1184–1185

    Mesh-Begriff(e) Antineoplastic Agents/adverse effects ; Antineoplastic Agents/therapeutic use ; Arsenic Trioxide ; Arsenicals/adverse effects ; Arsenicals/therapeutic use ; Carcinoma/diagnosis ; Carcinoma/etiology ; Carcinoma, Papillary ; Female ; Humans ; Leukemia, Promyelocytic, Acute/complications ; Leukemia, Promyelocytic, Acute/drug therapy ; Neoplasms, Second Primary/diagnosis ; Neoplasms, Second Primary/etiology ; Oxides/adverse effects ; Oxides/therapeutic use ; Thyroid Cancer, Papillary ; Thyroid Gland/metabolism ; Thyroid Neoplasms/diagnosis ; Thyroid Neoplasms/etiology ; Young Adult
    Chemische Substanzen Antineoplastic Agents ; Arsenicals ; Oxides ; Arsenic Trioxide (S7V92P67HO)
    Sprache Englisch
    Erscheinungsdatum 2013-09-23
    Erscheinungsland United States
    Dokumenttyp Case Reports ; Letter
    ZDB-ID 1042374-6
    ISSN 1029-2403 ; 1042-8194
    ISSN (online) 1029-2403
    ISSN 1042-8194
    DOI 10.3109/10428194.2013.837161
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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