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Jens Christian Jensenius

Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q

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Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q. / Zlatarova, A.S.; Rouseva, M.; Roumenina, L.T.; Gadjeva, M.; Kolev, M.; Dobrev, I.; Olova, N.; Ghai, R.; Jensenius, Jens Christian; Reid, K.B.; Kishore, U.; Kojouharova, M.S.

In: Biochemistry, Vol. 45, 2006, p. 9979-88.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Zlatarova, AS, Rouseva, M, Roumenina, LT, Gadjeva, M, Kolev, M, Dobrev, I, Olova, N, Ghai, R, Jensenius, JC, Reid, KB, Kishore, U & Kojouharova, MS 2006, 'Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q', Biochemistry, vol. 45, pp. 9979-88.

APA

Zlatarova, A. S., Rouseva, M., Roumenina, L. T., Gadjeva, M., Kolev, M., Dobrev, I., Olova, N., Ghai, R., Jensenius, J. C., Reid, K. B., Kishore, U., & Kojouharova, M. S. (2006). Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q. Biochemistry, 45, 9979-88.

CBE

Zlatarova AS, Rouseva M, Roumenina LT, Gadjeva M, Kolev M, Dobrev I, Olova N, Ghai R, Jensenius JC, Reid KB, Kishore U, Kojouharova MS. 2006. Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q. Biochemistry. 45:9979-88.

MLA

Vancouver

Zlatarova AS, Rouseva M, Roumenina LT, Gadjeva M, Kolev M, Dobrev I et al. Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q. Biochemistry. 2006;45:9979-88.

Author

Zlatarova, A.S. ; Rouseva, M. ; Roumenina, L.T. ; Gadjeva, M. ; Kolev, M. ; Dobrev, I. ; Olova, N. ; Ghai, R. ; Jensenius, Jens Christian ; Reid, K.B. ; Kishore, U. ; Kojouharova, M.S. / Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q. In: Biochemistry. 2006 ; Vol. 45. pp. 9979-88.

Bibtex

@article{d2cf6ea0c7d611dbbee902004c4f4f50,
title = "Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q",
abstract = "C1q is the first subcomponent of the classical complement pathway that binds antigen-bound IgG or IgM and initiates complement activation via association of serine proteases C1r and C1s. The globular domain of C1q (gC1q), which is the ligand-recognition domain, is a heterotrimeric structure composed of the C-terminal regions of A (ghA), B (ghB), and C (ghC) chains. The expression and functional characterization of ghA, ghB, and ghC modules have revealed that each chain has some structural and functional autonomy. Although a number of studies have tried to identify IgG-binding sites on the gC1q domain, no such attempt has been made to localize IgM-binding site. On the basis of the information available via the gC1q crystal structure, molecular modeling, mutational studies, and bioinformatics, we have generated a series of substitution mutants of ghA, ghB, and ghC and examined their interactions with IgM. The comparative analysis of IgM- and IgG-binding abilities of the mutants suggests that the IgG- and IgM-binding sites within the gC1q domain are different but may overlap. Whereas Arg(B108), Arg (B109), and Tyr(B175) mainly constitute the IgM-binding site, the residues Arg(B114), Arg(B129), Arg(B163), and His(B117) that have been shown to be central to IgG binding are not important for the C1q-IgM interaction. Given the location of Arg(B108), Arg (B109), and Tyr(B175) in the gC1q crystal structure, it is likely that C1q interacts with IgM via the top of the gC1q domain.",
author = "A.S. Zlatarova and M. Rouseva and L.T. Roumenina and M. Gadjeva and M. Kolev and I. Dobrev and N. Olova and R. Ghai and Jensenius, {Jens Christian} and K.B. Reid and U. Kishore and M.S. Kojouharova",
year = "2006",
language = "English",
volume = "45",
pages = "9979--88",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "ACS Publications",

}

RIS

TY - JOUR

T1 - Existence of different but overlapping IgG- and IgM-binding sties on the globular domain of human C1q

AU - Zlatarova, A.S.

AU - Rouseva, M.

AU - Roumenina, L.T.

AU - Gadjeva, M.

AU - Kolev, M.

AU - Dobrev, I.

AU - Olova, N.

AU - Ghai, R.

AU - Jensenius, Jens Christian

AU - Reid, K.B.

AU - Kishore, U.

AU - Kojouharova, M.S.

PY - 2006

Y1 - 2006

N2 - C1q is the first subcomponent of the classical complement pathway that binds antigen-bound IgG or IgM and initiates complement activation via association of serine proteases C1r and C1s. The globular domain of C1q (gC1q), which is the ligand-recognition domain, is a heterotrimeric structure composed of the C-terminal regions of A (ghA), B (ghB), and C (ghC) chains. The expression and functional characterization of ghA, ghB, and ghC modules have revealed that each chain has some structural and functional autonomy. Although a number of studies have tried to identify IgG-binding sites on the gC1q domain, no such attempt has been made to localize IgM-binding site. On the basis of the information available via the gC1q crystal structure, molecular modeling, mutational studies, and bioinformatics, we have generated a series of substitution mutants of ghA, ghB, and ghC and examined their interactions with IgM. The comparative analysis of IgM- and IgG-binding abilities of the mutants suggests that the IgG- and IgM-binding sites within the gC1q domain are different but may overlap. Whereas Arg(B108), Arg (B109), and Tyr(B175) mainly constitute the IgM-binding site, the residues Arg(B114), Arg(B129), Arg(B163), and His(B117) that have been shown to be central to IgG binding are not important for the C1q-IgM interaction. Given the location of Arg(B108), Arg (B109), and Tyr(B175) in the gC1q crystal structure, it is likely that C1q interacts with IgM via the top of the gC1q domain.

AB - C1q is the first subcomponent of the classical complement pathway that binds antigen-bound IgG or IgM and initiates complement activation via association of serine proteases C1r and C1s. The globular domain of C1q (gC1q), which is the ligand-recognition domain, is a heterotrimeric structure composed of the C-terminal regions of A (ghA), B (ghB), and C (ghC) chains. The expression and functional characterization of ghA, ghB, and ghC modules have revealed that each chain has some structural and functional autonomy. Although a number of studies have tried to identify IgG-binding sites on the gC1q domain, no such attempt has been made to localize IgM-binding site. On the basis of the information available via the gC1q crystal structure, molecular modeling, mutational studies, and bioinformatics, we have generated a series of substitution mutants of ghA, ghB, and ghC and examined their interactions with IgM. The comparative analysis of IgM- and IgG-binding abilities of the mutants suggests that the IgG- and IgM-binding sites within the gC1q domain are different but may overlap. Whereas Arg(B108), Arg (B109), and Tyr(B175) mainly constitute the IgM-binding site, the residues Arg(B114), Arg(B129), Arg(B163), and His(B117) that have been shown to be central to IgG binding are not important for the C1q-IgM interaction. Given the location of Arg(B108), Arg (B109), and Tyr(B175) in the gC1q crystal structure, it is likely that C1q interacts with IgM via the top of the gC1q domain.

M3 - Journal article

VL - 45

SP - 9979

EP - 9988

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

ER -