In the trafficking studies of active /inactive integrins, scientists usually employ conformation-specific antibodies (e.g., mAB13 for inactive integrin beta 1; HUTS-21 or 9EG7 for active beta 1) to track integrins of different conformations. I am confused and suspicious at the same time as to whether this method would still work whenever there is a conformation change. Taking alpha_5 beta_1 integrin (call it a5b1 for short) as an example, a common understanding of its trafficking process is that surface a5b1 binds with its ECM ligand fibronectin and gets activated. The ligand-bound, "active" a5b1 is internalized to early endosome, where the acidic environment triggers the dissociation of the bound ligand and hence a conformation change of a5b1 from active to inactive. The ligand-free, "inactive" a5b1 is then recycled back to membrane surface to form new focal adhesions with ECM. My question is: If the conformation-specific antibody, such as HUTS-21 or 9EG7, can only bind with integrins in specific form, would a conformation change (e.g., from active to inactive in the HUTS-21 or 9EG7-bound integrin beta1) trigger the detachment of these conformation-specific antibody? Or, would the HUTS-21 or 9FG7 antibody still remain bound but prevent conformation change of the antibody-bound integrin? Or, the HUTS-21 or 9FG7 antibody still remain bound and will not prevent integrin structural changes? Similarly, the mAb 13 antibody is known to bind only with "inactive" beta 1. Can the antibody still attach to the inactive integrin that is later become activated? What do you think the answer should be for the aformentioned different scenario? I would like to know your opinion.
My point is: if conformation-specific antibody cannot remain bound to the targeted integrins from the very beginning, then the antibody-based method won't be suitable to track integrins of different confromations, whenever integrins undergo conformation changes, which is bound to happen in most situations.
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