Humanization and Characterization of a Murine Monoclonal Neutralizing Antibody Against Human Adenovirus 7

Chen, Lei; Lu, Jiansheng; Wang, Rong; Huang, Ying; Yu, Yun-Zhou; Du, Peijun; Guo, Jiazheng; Wang, Xi; Jiang, Yujia; Cheng, Kexuan; Tang, Zheng; Yang, Zhixin

doi:10.2139/ssrn.4352953

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“…We checked the frequencies of amino acids in heavy chain position 93 using the abYsis software (Swindells et al, 2017). This database has previously been employed to examine the amino‐acid frequency at specific positions for the humanization of murine antibodies (Chen et al, 2023) and to optimize antibody framework sequences (Douillard et al, 2019). The differences in residue features across various organisms were also analyzed in a previous study (Mendoza et al, 2020).…”

Section: Discussionmentioning

confidence: 99%

Conformational features and interaction mechanisms of V_HH antibodies with β‐hairpin CDR3: A case of Nb8‐HigB2 interaction

Yamamoto,

Nagatoishi,

Matsunaga

et al. 2023

Protein Science

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Abstractβ‐hairpin conformation is regarded as an important basic motif to form and regulate protein‐protein interactions. Single‐domain VHH antibodies are potential therapeutic and diagnostic tools, and the third complementarity‐determining regions of the heavy chains (CDR3s) of these antibodies are critical for antigen recognition. Although the sequences and conformations of the CDR3s are diverse, CDR3s sometimes adopt β‐hairpin conformations. However, characteristic features and interaction mechanisms of β‐hairpin CDR3s remain to be fully elucidated. In this study, we investigated the molecular recognition of the anti‐HigB2 VHH antibody Nb8, which has a CDR3 that forms a β‐hairpin conformation. The interaction was analyzed by evaluation of alanine‐scanning mutants, molecular dynamics simulations, and hydrogen/deuterium exchange mass spectrometry. These experiments demonstrated that positions 93 and 94 (Chothia numbering) in framework region 3, which is right outside CDR3 by definition, play pivotal roles in maintaining structural stability and binding properties of Nb8. These findings will facilitate design and optimization of single‐domain antibodies.This article is protected by copyright. All rights reserved.

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Section: Discussionmentioning

confidence: 99%

Conformational features and interaction mechanisms of V_HH antibodies with β‐hairpin CDR3: A case of Nb8‐HigB2 interaction

Yamamoto,

Nagatoishi,

Matsunaga

et al. 2023

Protein Science

View full text Add to dashboard Cite

show abstract

Humanization and Characterization of a Murine Monoclonal Neutralizing Antibody Against Human Adenovirus 7

Cited by 1 publication

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Conformational features and interaction mechanisms of V_HH antibodies with β‐hairpin CDR3: A case of Nb8‐HigB2 interaction

Conformational features and interaction mechanisms of V_HH antibodies with β‐hairpin CDR3: A case of Nb8‐HigB2 interaction

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Humanization and Characterization of a Murine Monoclonal Neutralizing Antibody Against Human Adenovirus 7

Cited by 1 publication

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Conformational features and interaction mechanisms of VHH antibodies with β‐hairpin CDR3: A case of Nb8‐HigB2 interaction

Conformational features and interaction mechanisms of VHH antibodies with β‐hairpin CDR3: A case of Nb8‐HigB2 interaction

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Conformational features and interaction mechanisms of V_HH antibodies with β‐hairpin CDR3: A case of Nb8‐HigB2 interaction

Conformational features and interaction mechanisms of V_HH antibodies with β‐hairpin CDR3: A case of Nb8‐HigB2 interaction