Jack Leonard Strominger (born August 7, 1925)[1] is the Higgins Professor of Biochemistry at Harvard University, specializing in the structure and function of human histocompatibility proteins and their role in disease.
In 1951, during the Korean War the United States Navy called him back into service to be stationed at a hospital in Bangkok, Thailand.
At Washington University in St. Louis, he discovered that uridine nucleotide that accumulated in the penicillin-treated bacterium staphylococcus aureus was a precursor of the bacterial cell wall.
There, with Donald J. Tipper in 1965, he demonstrated the mechanism of action by which antibiotic penicillins kill bacteria by inhibiting the completion of the synthesis of structural components of bacterial cell walls known as peptidoglycans.
Penicillins specifically inhibit the activity of enzymes that are needed for the cross-linking of peptidoglycans during the final step in cell wall biosynthesis.
These antibiotics do this by binding to the group of enzymes known as Penicillin-binding proteins using a chemical structure found on penicillin molecules known as a β-lactam ring.
Later, Stan Nathenson worked with Davies to characterize transplantation antigens and discovered that they could be solubilized from the surfaces of cells by the protease papain.
[3] At that time, the institute's director was Emil Frei who had been a classmate with Strominger at Yale Medical School.
The MHC is a large locus on vertebrate DNA containing a set of closely linked polymorphic genes that code for cell membrane-embedded external surface proteins essential for the adaptive immune system.