WILLIAM MARSH BALDWIN, M.D.
Medical Practice at Wolfe St, Baltimore, MD

6140472, Oct 31, 2000

Nov 30, 1998

9/201075

Ariella M. Rosengard - Gladwyne PA
Joseph M. Ahearn - Baltimore MD
Alfred P. Sanfilippo - Baltimore MD
William M. Baldwin - Baltimore MD

The Johns Hopkins University School of Medicine - Baltimore MD

C07K 1646

5303873

Disclosed are chimeric proteins that are useful for inhibiting complement. The chimeric protein termed VCPFc is a fusion protein in which (i) an immunoglobulin Fc region is fused to (ii) a polypeptide that comprises a portion of a vaccinia virus complement control protein which binds complement components C4b and C3b, but not iC3b rosettes. This protein can be used in xenograft transplantation methods (e. g. , by treating the donor mammal or organ) and in methods for treating complement-mediated disorders (e. g. , inflammation) generally. In a second chimeric protein, a transmembrane anchoring domain is fused to a polypeptide that comprises a portion of a vaccinia virus complement control protein which binds complement components C4b and C3b, but not iC3b rosettes. The transmembrane anchoring domain can be, for example, short consensus regions 3 through 15 of human complement receptor 2 protein. Expression of the transmembrane-anchored fusion protein in a transgenic animal provides a well-suited organ donor for xenograft transplantation.

5679345, Oct 21, 1997

Jun 2, 1994

8/253279

Alfred P. Sanfilippo - Baltimore MD
William M. Baldwin - Baltimore MD
Robert B. Brauer - Baltimore MD

The Johns Hopkins University - Baltimore MD

C07K 1618, C07K 14435, A61K 39395, A61K 3817

4241301

Interference with formation of the complement-based membrane attack complex (MAC) will mitigate or even prevent tissue injury associated with the effects of complement in inflammation and graft rejection. Passive treatment of xenograft recipients at the time of and after transplantation with antibody against C-6, which interrupts the sequence of binding steps that form MAC, has been observed to suppress hyperacute xenograft rejection with no adverse signs or symptoms in the xenograft recipient. The present invention provides a method for interfering with MAC formation in transplant recipients, by administering compounds which interrupt one or more of the binding reactions between C5b and C6-C9, so that the MAC cannot form.

5843778, Dec 1, 1998

Jun 13, 1997

8/874978

Ariella M. Rosengard - Gladwyne PA
Joseph M. Ahearn - Baltimore MD
Alfred P. Sanfilippo - Baltimore MD
William M. Baldwin - Baltimore MD

The Johns Hopkins University School of Medicine - Baltimore MD

C12P 2100, C12N 1539, C12N 510, C07H 2104

435325

Disclosed are chimeric proteins that are useful for inhibiting complement. The chimeric protein termed VCPFc is a fusion protein in which (i) an immunoglobulin Fc region is fused to (ii) a polypeptide that comprises a portion of a vaccinia virus complement control protein which binds complement components C4b and C3b, but not iC3b rosettes. This protein can be use in xenograft transplantation methods (e. g. , by treating the donor mammal or organ) and in methods for treating complement-mediated disorders (e. g. , inflammation) generally. In a second chimeric protein, a transmembrane anchoring domain is fused to a polypeptide that comprises a portion of a vaccinia virus complement control protein which binds complement components C4b and C3b, but not iC3b rosettes. The transmembrane anchoring domain can be, for example, short consensus regions 3 through 15 of human complement receptor 2 protein. Expression of the transmembrane-anchored fusion protein in a transgenic animal provides a well-suited organ donor for xenograft transplantation.