Jack L. Strominger

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Jack L. Strominger
Born (1925-08-07) August 7, 1925 (age 98)
New York City, US
Alma mater
Doctoral studentsTimothy A. Springer
Hidde Ploegh
Matthew F. Mescher
David J. Waxman
Joel N. H. Stern
Brandy L. Houser
Leonardo M.R. Ferreira
Peter Cresswell

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. He won the Albert Lasker Award for Basic Medical Research in 1995.[2][3]

Early life and education

Strominger was born in

Yale Medical School.[4]

Career

After graduation he joined the faculty at the

bacterial cell wall
.

Strominger joined the

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. β-lactam imitates the naturally occurring acyl-D-alanyl-D-alanine substrate for the enzymes.[5]

He joined the Harvard faculty in 1968 to work in the biochemistry and molecular biology department specializing in microbial biochemistry, with a small portion of his time being devoted to organ transplantation biology. Knowledge was scarce with respect to the mechanisms of allograft rejection. There was none for the transplantation antigens. Graft acceptance or rejection was only hinted at through previous knowledge of Blood type erythrocyte transfusion. In the mid-1960's, Allan Davies from the United Kingdom had discovered a number of the 3,6-dideoxyhexoses that could be utilized to distinguish bacterial surfaces. Davies speculated that the specificity of transplantation antigen might also be determined by cell surface arrangements of sugars. 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.[6]

In 1974, Stominger became a member of the

polymorphic genes that code for cell membrane-embedded external surface proteins essential for the adaptive immune system. These cell surface proteins are called MHC molecules. Together with X-ray diffraction protein crystallographer Don Wiley, Strominger (who supplied biological cell culture systems and proteins) solved the chemical structures and three-dimensional structures of several MHC proteins, and further, solved the three-dimensional structures of the chemical complexes of these proteins during their peptide substrate interactions.[2] Early work, elucidated the three-dimensional structures of the human class I MHC molecules of HLA-A2, HLA-A68, and HLA-B27. Ultimately, papain-solubilized fragments of the human class II MHC antigens HLA-DR1, HLA-DR2, HLA-DR3, HLA-DR4, HLA-DR7, and HLA-DR8 were purified from homozygous human B lymphoblastoid cell lines
and crystals were grown for diffraction studies.

Awards

Strominger was the first recipient of the

National Institute of Medicine in 1975.[10][11] He was elected to the American Philosophical Society in 1994.[12] In 1999, he received the Japan Prize.[1]

Personal life

Strominger married Ann in 1951. She died in 2017. Their children are physicist Andrew Strominger,[13] Ethan Strominger and Paul Strominger.

References

  1. ^ a b Dr. Jack L. Strominger. japanprize.jp
  2. ^ a b "Lasker Foundation – 1995 Basic Medical Research Award". Lasker Foundation. 1995. Retrieved 1 February 2010.
  3. ^ a b "Jack Leonard Strominger". The Complete Marquis Who's Who (R) Biographies. Marquis Who's Who LLC. 6 November 2009.
  4. PMID 16551242
    .
  5. .
  6. .
  7. ^ "Selman A. Waksman Award in Microbiology". National Academy of Sciences. Archived from the original on 12 January 2011. Retrieved 15 February 2011.
  8. American Academy of Achievement
    .
  9. ^ "Jack Leonard Strominger". American Academy of Arts & Sciences. Retrieved 2022-02-10.
  10. ^ "National Academy of Sciences: Directory Entry". Retrieved 1 February 2010.
  11. ^ "Institute of Medicine: Directory". Institute of Medicine, National Academy of Science. Archived from the original on 11 December 2012. Retrieved 1 February 2010.
  12. ^ "APS Member History". search.amphilsoc.org. Retrieved 2022-02-10.
  13. ^ "Still wrestling with big questions". Harvard News. 6 January 2020.

Further reading

External links