Methods for preparing and using multichaperone-antigen complexes
AssigneeAgenus Inc.
InventorsKenneth P. Leclair, Andrew J. Tomlinson
Life of this patent
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Abstract
The present invention relates to methods for preparing and using multichaperone-antigen complexes. The present invention uses HOP affinity molecules in affinity methods to isolate multichaperone (multi-HSP)-antigen complexes. Such complexes have use in therapy.
Claims52
A method for preparing multichaperone-antigen complexes comprising:
- (a) contacting a biological sample with a solid phase to which HOP affinity molecules are covalently bound, under conditions such that multichaperone-antigen complexes in the biological sample bind said HOP affinity molecules, wherein the HOP affinity molecules comprise HOP TPR1, having an amino acid sequence as set forth in SEQ ID NO:
- 1, HOP TPR2a, having an amino acid sequence as set forth in SEQ ID NO:
- 2, HOP TPR1/2a, having an amino acid sequence as set forth in SEQ ID NO:
- 3, or a combination or variant of any one or more of the foregoing, wherein a variant is a HOP affinity molecule defined above containing deletions, insertions, substitutions or other modifications relative to the native HOP affinity molecule sequence and retains the specificity of the native HOP affinity molecule to bind heat shock proteins;
- (b) removing unbound components in the biological sample away from the solid phase;
- (c) eluting multichaperone-antigen complexes from the solid phase;
- and
- (d) recovering the eluted multichaperone-antigen complexes.
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A composition comprising mammalian HOP affinity molecules covalently bound to a solid phase, wherein the HOP affinity molecules comprise a HOP affinity fragment or variant thereof selected from the group consisting of HOP TPR1 or a variant thereof, HOP TPR2a or a variant thereof, HOP TPR 1/2a or a variant thereof, and a combination of any one or more of the foregoing, wherein a variant is a HOP affinity molecule defined above containing deletions, insertions, substitutions or other modifications relative to the native HOP affinity molecule sequence and retains the specificity of the native HOP affinity molecule to bind heat shock proteins.
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Dependencies are inferred from the claim text.