Leporid immunoglobulin G shows evidence of strong selective pressure on the hinge and CH3 domains

Ana Pinheiro, Jenny M. Woof, Tereza Almeida, Joana Abrantes, Paulo C. Alves, Christian Gortázar, Pedro J. Esteves (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    13 Citations (Scopus)

    Abstract

    Immunoglobulin G (IgG) is the predominant serum immunoglobulin and has the longest serum half-life of all the antibody classes. The European rabbit IgG has been of significant importance in immunological research, and is therefore well characterized. However, the IgG of other leporids has been disregarded. To evaluate the evolution of this gene in leporids, we sequenced the complete IGHG for six other genera: Bunolagus, Brachylagus, Lepus, Pentalagus, Romerolagus and Sylvilagus. The newly sequenced leporid IGHG gene has an organization and structure similar to that of the European rabbit IgG. A gradient in leporid IgG constant domain diversity was observed, with the CH1 being the most conserved and the CH3 the most variable domain. Positive selection was found to be acting on all constant domains, but with a greater incidence in the CH3 domain, where a cluster of three positively selected sites was identified. In the hinge region, only three polymorphic positions were observed. The same hinge length was observed for all leporids. Unlike the variation observed for the European rabbit, all 11 Lepus species studied share exactly the same hinge motif, suggesting its maintenance as a result of an advantageous structure or conformation.
    Original languageEnglish
    Article number140088
    Number of pages9
    JournalOpen Biology
    Volume4
    Issue number9
    DOIs
    Publication statusPublished - Sep 2014

    Fingerprint

    Hinges
    Immunoglobulin G
    Hares
    Rabbits
    Genes
    Immunoglobulin Isotypes
    Serum
    Half-Life
    Conformations
    Immunoglobulins
    Maintenance
    Incidence
    Research

    Cite this

    Pinheiro, A., Woof, J. M., Almeida, T., Abrantes, J., Alves, P. C., Gortázar, C., & Esteves, P. J. (2014). Leporid immunoglobulin G shows evidence of strong selective pressure on the hinge and CH3 domains. Open Biology, 4(9), [140088]. https://doi.org/10.1098/rsob.140088
    Pinheiro, Ana ; Woof, Jenny M. ; Almeida, Tereza ; Abrantes, Joana ; Alves, Paulo C. ; Gortázar, Christian ; Esteves, Pedro J. / Leporid immunoglobulin G shows evidence of strong selective pressure on the hinge and CH3 domains. In: Open Biology. 2014 ; Vol. 4, No. 9.
    @article{d12deb4585184caaa79cc8203a5f4235,
    title = "Leporid immunoglobulin G shows evidence of strong selective pressure on the hinge and CH3 domains",
    abstract = "Immunoglobulin G (IgG) is the predominant serum immunoglobulin and has the longest serum half-life of all the antibody classes. The European rabbit IgG has been of significant importance in immunological research, and is therefore well characterized. However, the IgG of other leporids has been disregarded. To evaluate the evolution of this gene in leporids, we sequenced the complete IGHG for six other genera: Bunolagus, Brachylagus, Lepus, Pentalagus, Romerolagus and Sylvilagus. The newly sequenced leporid IGHG gene has an organization and structure similar to that of the European rabbit IgG. A gradient in leporid IgG constant domain diversity was observed, with the CH1 being the most conserved and the CH3 the most variable domain. Positive selection was found to be acting on all constant domains, but with a greater incidence in the CH3 domain, where a cluster of three positively selected sites was identified. In the hinge region, only three polymorphic positions were observed. The same hinge length was observed for all leporids. Unlike the variation observed for the European rabbit, all 11 Lepus species studied share exactly the same hinge motif, suggesting its maintenance as a result of an advantageous structure or conformation.",
    author = "Ana Pinheiro and Woof, {Jenny M.} and Tereza Almeida and Joana Abrantes and Alves, {Paulo C.} and Christian Gort{\'a}zar and Esteves, {Pedro J.}",
    year = "2014",
    month = "9",
    doi = "10.1098/rsob.140088",
    language = "English",
    volume = "4",
    journal = "Open Biology",
    issn = "2046-2441",
    publisher = "The Royal Society",
    number = "9",

    }

    Pinheiro, A, Woof, JM, Almeida, T, Abrantes, J, Alves, PC, Gortázar, C & Esteves, PJ 2014, 'Leporid immunoglobulin G shows evidence of strong selective pressure on the hinge and CH3 domains', Open Biology, vol. 4, no. 9, 140088. https://doi.org/10.1098/rsob.140088

    Leporid immunoglobulin G shows evidence of strong selective pressure on the hinge and CH3 domains. / Pinheiro, Ana; Woof, Jenny M.; Almeida, Tereza; Abrantes, Joana; Alves, Paulo C.; Gortázar, Christian; Esteves, Pedro J. (Lead / Corresponding author).

    In: Open Biology, Vol. 4, No. 9, 140088, 09.2014.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Leporid immunoglobulin G shows evidence of strong selective pressure on the hinge and CH3 domains

    AU - Pinheiro, Ana

    AU - Woof, Jenny M.

    AU - Almeida, Tereza

    AU - Abrantes, Joana

    AU - Alves, Paulo C.

    AU - Gortázar, Christian

    AU - Esteves, Pedro J.

    PY - 2014/9

    Y1 - 2014/9

    N2 - Immunoglobulin G (IgG) is the predominant serum immunoglobulin and has the longest serum half-life of all the antibody classes. The European rabbit IgG has been of significant importance in immunological research, and is therefore well characterized. However, the IgG of other leporids has been disregarded. To evaluate the evolution of this gene in leporids, we sequenced the complete IGHG for six other genera: Bunolagus, Brachylagus, Lepus, Pentalagus, Romerolagus and Sylvilagus. The newly sequenced leporid IGHG gene has an organization and structure similar to that of the European rabbit IgG. A gradient in leporid IgG constant domain diversity was observed, with the CH1 being the most conserved and the CH3 the most variable domain. Positive selection was found to be acting on all constant domains, but with a greater incidence in the CH3 domain, where a cluster of three positively selected sites was identified. In the hinge region, only three polymorphic positions were observed. The same hinge length was observed for all leporids. Unlike the variation observed for the European rabbit, all 11 Lepus species studied share exactly the same hinge motif, suggesting its maintenance as a result of an advantageous structure or conformation.

    AB - Immunoglobulin G (IgG) is the predominant serum immunoglobulin and has the longest serum half-life of all the antibody classes. The European rabbit IgG has been of significant importance in immunological research, and is therefore well characterized. However, the IgG of other leporids has been disregarded. To evaluate the evolution of this gene in leporids, we sequenced the complete IGHG for six other genera: Bunolagus, Brachylagus, Lepus, Pentalagus, Romerolagus and Sylvilagus. The newly sequenced leporid IGHG gene has an organization and structure similar to that of the European rabbit IgG. A gradient in leporid IgG constant domain diversity was observed, with the CH1 being the most conserved and the CH3 the most variable domain. Positive selection was found to be acting on all constant domains, but with a greater incidence in the CH3 domain, where a cluster of three positively selected sites was identified. In the hinge region, only three polymorphic positions were observed. The same hinge length was observed for all leporids. Unlike the variation observed for the European rabbit, all 11 Lepus species studied share exactly the same hinge motif, suggesting its maintenance as a result of an advantageous structure or conformation.

    U2 - 10.1098/rsob.140088

    DO - 10.1098/rsob.140088

    M3 - Article

    C2 - 25185680

    VL - 4

    JO - Open Biology

    JF - Open Biology

    SN - 2046-2441

    IS - 9

    M1 - 140088

    ER -