Herpes simplex type 1-induced Fc receptor binds to the Cgamma2-Cgamma3 interface region of IgG in the area that binds staphylococcal protein A
(1989) In Immunology 66(1). p.8-13- Abstract
- The binding site of immunoglobulin G (IgG) to herpes simplex virus (HSV) type 1-induced Fc receptor was investigated using human IgG Fc intermediate (Fc(i)) fragments, fragment D of staphylococcal protein A (SPA) and chemically modified human IgG. Human IgG Fc(i) fragment composed of one Cgamma2 and two Cgamma3 domains, bound strongly to HSV-1-infected cells. Fragment D, a monovalent subunit of SPA, inhibited the binding of radiolabelled human IgG Fc fragments to the HSV Fc receptor. Reductively methylated human IgG reacted equally well to HSV-infected cells, as did chemically unmodified IgG in contrast to N-acetylimidazole-modified and diethylpyrocarbonate-modifed human IgG, which were unreactive. These results suggest a similar binding... (More)
- The binding site of immunoglobulin G (IgG) to herpes simplex virus (HSV) type 1-induced Fc receptor was investigated using human IgG Fc intermediate (Fc(i)) fragments, fragment D of staphylococcal protein A (SPA) and chemically modified human IgG. Human IgG Fc(i) fragment composed of one Cgamma2 and two Cgamma3 domains, bound strongly to HSV-1-infected cells. Fragment D, a monovalent subunit of SPA, inhibited the binding of radiolabelled human IgG Fc fragments to the HSV Fc receptor. Reductively methylated human IgG reacted equally well to HSV-infected cells, as did chemically unmodified IgG in contrast to N-acetylimidazole-modified and diethylpyrocarbonate-modifed human IgG, which were unreactive. These results suggest a similar binding site on human IgG for SPA and the HSV-1 Fc receptor with involvement of the amino acid residues Tyr and His but not Lys. The similarities of binding sites on the IgG molecule for the HSV-1 Fc receptor and rheumatoid factors (RF) may be important for understanding the mechanism of RF production in rheumatoid arthritis or other disease states. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1104530
- author
- Johansson, Hugo LU ; Nardella, F A ; Sjöquist, J ; Schröder, A K and Christensen, P
- organization
- publishing date
- 1989
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Immunology
- volume
- 66
- issue
- 1
- pages
- 8 - 13
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:15493255
- scopus:0024495125
- ISSN
- 0019-2805
- language
- English
- LU publication?
- yes
- id
- f78f3e83-773d-4419-acde-6c9efc7ddc01 (old id 1104530)
- alternative location
- http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1385112&blobtype=pdf
- date added to LUP
- 2016-04-01 12:06:30
- date last changed
- 2021-01-03 06:17:09
@article{f78f3e83-773d-4419-acde-6c9efc7ddc01, abstract = {{The binding site of immunoglobulin G (IgG) to herpes simplex virus (HSV) type 1-induced Fc receptor was investigated using human IgG Fc intermediate (Fc(i)) fragments, fragment D of staphylococcal protein A (SPA) and chemically modified human IgG. Human IgG Fc(i) fragment composed of one Cgamma2 and two Cgamma3 domains, bound strongly to HSV-1-infected cells. Fragment D, a monovalent subunit of SPA, inhibited the binding of radiolabelled human IgG Fc fragments to the HSV Fc receptor. Reductively methylated human IgG reacted equally well to HSV-infected cells, as did chemically unmodified IgG in contrast to N-acetylimidazole-modified and diethylpyrocarbonate-modifed human IgG, which were unreactive. These results suggest a similar binding site on human IgG for SPA and the HSV-1 Fc receptor with involvement of the amino acid residues Tyr and His but not Lys. The similarities of binding sites on the IgG molecule for the HSV-1 Fc receptor and rheumatoid factors (RF) may be important for understanding the mechanism of RF production in rheumatoid arthritis or other disease states.}}, author = {{Johansson, Hugo and Nardella, F A and Sjöquist, J and Schröder, A K and Christensen, P}}, issn = {{0019-2805}}, language = {{eng}}, number = {{1}}, pages = {{8--13}}, publisher = {{Wiley-Blackwell}}, series = {{Immunology}}, title = {{Herpes simplex type 1-induced Fc receptor binds to the Cgamma2-Cgamma3 interface region of IgG in the area that binds staphylococcal protein A}}, url = {{http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1385112&blobtype=pdf}}, volume = {{66}}, year = {{1989}}, }