Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways

Yohannes T. Ghebremariam; Odutayo O. Odunuga; Kristen Janse; Girish J. Kotwal

doi:10.1196/annals.1352.024

Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways

Yohannes T. Ghebremariam
, Odutayo O. Odunuga
, Kristen Janse
, Girish J. Kotwal

Research output: Contribution to journal › Article › peer-review

Original language	English
Pages (from-to)	113-122
Number of pages	10
Journal	Annals of the New York Academy of Sciences
Volume	1056
DOIs	https://doi.org/10.1196/annals.1352.024
State	Published - 2005
Externally published	Yes

ASJC Scopus Subject Areas

General Neuroscience
General Biochemistry,Genetics and Molecular Biology
History and Philosophy of Science

Keywords

100-Fold potency
Complement
Heparin
Humanized rVCPs
Site-directed mutagenesis
rVCP

Access to Document

10.1196/annals.1352.024

Cite this

Ghebremariam, Y. T., Odunuga, O. O., Janse, K., & Kotwal, G. J. (2005). Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways. Annals of the New York Academy of Sciences, 1056, 113-122. https://doi.org/10.1196/annals.1352.024

Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways. / Ghebremariam, Yohannes T.; Odunuga, Odutayo O.; Janse, Kristen et al.
In: Annals of the New York Academy of Sciences, Vol. 1056, 2005, p. 113-122.

Research output: Contribution to journal › Article › peer-review

Ghebremariam, YT, Odunuga, OO, Janse, K & Kotwal, GJ 2005, 'Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways', Annals of the New York Academy of Sciences, vol. 1056, pp. 113-122. https://doi.org/10.1196/annals.1352.024

Ghebremariam YT, Odunuga OO, Janse K, Kotwal GJ. Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways. Annals of the New York Academy of Sciences. 2005;1056:113-122. doi: 10.1196/annals.1352.024

Ghebremariam, Yohannes T. ; Odunuga, Odutayo O. ; Janse, Kristen et al. / Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways. In: Annals of the New York Academy of Sciences. 2005 ; Vol. 1056. pp. 113-122.

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title = "Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways",

keywords = "100-Fold potency, Complement, Heparin, Humanized rVCPs, Site-directed mutagenesis, rVCP",

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T1 - Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways

AU - Ghebremariam, Yohannes T.

AU - Odunuga, Odutayo O.

AU - Janse, Kristen

AU - Kotwal, Girish J.

PY - 2005

Y1 - 2005

KW - 100-Fold potency

KW - Complement

KW - Heparin

KW - Humanized rVCPs

KW - Site-directed mutagenesis

KW - rVCP

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DO - 10.1196/annals.1352.024

M3 - Article

C2 - 16387681

AN - SCOPUS:29744456997

SN - 0077-8923

VL - 1056

SP - 113

EP - 122

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

ER -

Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways

ASJC Scopus Subject Areas

Keywords

Access to Document

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