Structural Studies in Solution of the Recombinant N-Terminal Pair of Short Consensus/Complement Repeat Domains of Complement Receptor Type 2 (CR2/CD21) and Interactions with Its Ligand C3dg†

Biochemistry ◽  
2001 ◽  
Vol 40 (20) ◽  
pp. 5931-5941 ◽  
Author(s):  
Joel M. Guthridge ◽  
Jonathan K. Rakstang ◽  
Kendra A. Young ◽  
Justin Hinshelwood ◽  
Mohammed Aslam ◽  
...  
Keyword(s):  
Receptor Type ◽  
Complement Receptor ◽  
Structural Studies ◽  
Complement Receptor Type ◽  
Terminal Pair

scholarly journals The generation of active fragments of complement receptor type 2 by trypsin digestion

FEBS Letters ◽  
1985 ◽  
Vol 189 (2) ◽  
pp. 195-201 ◽  
Author(s):  
Kingsley Micklem ◽  
Edith Sim ◽  
Robert B. Sim
Keyword(s):  
Trypsin Digestion ◽  
Receptor Type ◽  
Complement Receptor ◽  
Complement Receptor Type ◽  
Active Fragments

Modulation of murine complement receptor type 2 (CR2/CD21) ectodomain shedding by its cytoplasmic domain

2008 ◽  
Vol 45 (8) ◽  
pp. 2127-2137 ◽  
Author(s):  
Melanie M. Hoefer ◽  
Annette Aichem ◽  
Andrew M. Knight ◽  
Harald Illges
Keyword(s):  
Cytoplasmic Domain ◽  
Receptor Type ◽  
Complement Receptor ◽  
Ectodomain Shedding ◽  
Complement Receptor Type

The 15 SCR Flexible Extracellular Domains of Human Complement Receptor Type 2 can Mediate Multiple Ligand and Antigen Interactions

2006 ◽  
Vol 362 (5) ◽  
pp. 1132-1147 ◽  
Author(s):  
Hannah E. Gilbert ◽  
Rengasamy Asokan ◽  
V. Michael Holers ◽  
Stephen J. Perkins
Keyword(s):  
Receptor Type ◽  
Complement Receptor ◽  
Human Complement ◽  
Complement Receptor Type ◽  
Extracellular Domains ◽  
Multiple Ligand

scholarly journals Identification of murine complement receptor type 2.

1989 ◽  
Vol 86 (1) ◽  
pp. 242-246 ◽  
Author(s):  
J. D. Fingeroth ◽  
M. A. Benedict ◽  
D. N. Levy ◽  
J. L. Strominger
Keyword(s):  
Receptor Type ◽  
Complement Receptor ◽  
Complement Receptor Type

Structure of complement receptor type 2 (CR2, CD21) on HTLV-I transformed cell lines

1995 ◽  
Vol 121 (S1) ◽  
pp. S32-S32
Author(s):  
W. M. Prodinger ◽  
C. Larcher ◽  
M. Schwendinger ◽  
M. P. Dierich
Keyword(s):  
Cell Lines ◽  
Receptor Type ◽  
Complement Receptor ◽  
Complement Receptor Type ◽  
Transformed Cell ◽  
Transformed Cell Lines

scholarly journals A new mouse anti-mouse complement receptor type 2 and 1 (CR2/CR1) monoclonal antibody as a tool to study receptor involvement in chronic models of immune responses and disease

2015 ◽  
Vol 63 (2) ◽  
pp. 479-488 ◽  
Author(s):  
Liudmila Kulik ◽  
Finnegan B. Hewitt ◽  
Van C. Willis ◽  
Rosa Rodriguez ◽  
Stephen Tomlinson ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Immune Responses ◽  
Receptor Type ◽  
Complement Receptor ◽  
Complement Receptor Type ◽  
Chronic Models

scholarly journals Molecular Basis of the Interaction between Complement Receptor Type 2 (CR2/CD21) and Epstein-Barr Virus Glycoprotein gp350

2008 ◽  
Vol 82 (22) ◽  
pp. 11217-11227 ◽  
Author(s):  
Kendra A. Young ◽  
Andrew P. Herbert ◽  
Paul N. Barlow ◽  
V. Michael Holers ◽  
Jonathan P. Hannan
Keyword(s):  
Epstein Barr Virus ◽  
Receptor Type ◽  
Complement Receptor ◽  
Wild Type ◽  
Virus Glycoprotein ◽  
Complement Receptor Type ◽  
Barr Virus ◽  
Epstein Barr ◽  
Mutant Forms

ABSTRACT The binding of the Epstein-Barr virus glycoprotein gp350 by complement receptor type 2 (CR2) is critical for viral attachment to B lymphocytes. We set out to test hypotheses regarding the molecular nature of this interaction by developing an enzyme-linked immunosorbent assay (ELISA) for the efficient analysis of the gp350-CR2 interaction by utilizing wild-type and mutant forms of recombinant gp350 and also of the CR2 N-terminal domains SCR1 and SCR2 (designated CR2 SCR1-2). To delineate the CR2-binding site on gp350, we generated 17 gp350 single-site substitutions targeting an area of gp350 that has been broadly implicated in the binding of both CR2 and the major inhibitory anti-gp350 monoclonal antibody (MAb) 72A1. These site-directed mutations identified a novel negatively charged CR2-binding surface described by residues Glu-21, Asp-22, Glu-155, Asp-208, Glu-210, and Asp-296. We also identified gp350 amino acid residues involved in non-charge-dependent interactions with CR2, including Tyr-151, Ile-160, and Trp-162. These data were supported by experiments in which phycoerythrin-conjugated wild-type and mutant forms of gp350 were incubated with CR2-expressing K562 cells and binding was assessed by flow cytometry. The ELISA was further utilized to identify several positively charged residues (Arg-13, Arg-28, Arg-36, Lys-41, Lys-57, Lys-67, Arg-83, and Arg-89) within SCR1-2 of CR2 that are involved in the binding interaction with gp350. These experiments allowed a comparison of those CR2 residues that are important for binding gp350 to those that define the epitope for an effective inhibitory anti-CR2 MAb, 171 (Asn-11, Arg-13, Ser-32, Thr-34, Arg-36, and Tyr-64). The mutagenesis data were used to calculate a model of the CR2-gp350 complex using the soft-docking program HADDOCK.

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