Abstract：
:The cell surface co-stimulatory protein CD154 (CD40L) is a target for monoclonal antibody (mAb) inhibitors of T-cell mediated immune diseases. This protein, like most other members of the TNF ligand family, forms homotrimeric complexes on the cell surface and in solution, with a three-fold axis of symmetry. We find that several different anti-CD154 monoclonal antibodies form distinctive complexes with soluble CD154. These soluble complexes have been analyzed using size exclusion chromatography, static and dynamic light scattering, and electron microscopy and shown to consist of caged structures of various geometries. The cell surface complexes have been analyzed by confocal microscopy and, depending on the mAb, remain as small, separate complexes or form large aggregates. The formation of these complexes in solution is likely to have an impact on measures of affinity, while the cell surface complexes could affect binding potency and provoke other biological effects.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Ferrant JL,Wilson CA,Benjamin CD,Hess DM,Hsu YM,Karpusas M,Roux KH,Taylor FRdoi
10.1016/s0161-5890(02)00045-7subject
Has Abstractpub_date
2002-09-01 00:00:00pages
77-84issue
1-2eissn
0161-5890issn
1872-9142pii
S0161589002000457journal_volume
39pub_type
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pub_type： 杂志文章
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pub_type： 杂志文章
doi：10.1016/0161-5890(87)90068-x
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pub_type： 杂志文章
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更新日期：1998-11-01 00:00:00
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pub_type： 杂志文章
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pub_type： 杂志文章
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journal_title：Molecular immunology
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