MYRON E ESSEX
Veterinary in Sharon, MA

6531574, Mar 11, 2003

Jan 24, 1995

08/378872

Myron E. Essex - Sharon MA
Phyllis J. Kanki - Carlisle MA

President and Fellows of Harvard College - Cambridge MA

C07K 100

530350, 435 41, 435 711, 4352351, 435236, 435239, 435372, 530395, 530826

A substantially pure polypeptide having at least one antigenic determinant that is substantially identical to an antigenic determinant of a protein from a cell line infected with a specified virus that has been deposited with the ATCC, the protein being selected from: a) a glycoprotein having a molecular weight (m. w. ) of about 160,000 daltons; a glycoprotein having a m. w. of about 120,000 daltons; a gag protein having a m. w. of about 55,000 daltons; a gag protein having a m. w. of about 24,000 daltons; and a glycoprotein having a m. w. of about 32,000 daltons. Also disclosed are various methods of immunoassay using that peptide or antibodies raised to it. Finally, immunoassays for simian specimens are disclosed using peptides that are immunologically cross-reactive with the above-described peptide, or antibodies thereto.

4725669, Feb 16, 1988

Nov 9, 1984

6/670361

Myron E. Essex - Sharon MA
Tun-Hou Lee - Stockholm, SE

President and Fellows of Harvard College - Cambridge MA

C07C10352, C07G 700

530322

A first glycoprotein having a molecular weight of approximately 120,000 daltons in the H9/HTLV-III cell line, of which approximately 90,000 daltons is the unglycosylated moiety, is obtained from cells infected with human T-cell leukemia virus, type III. A second glycoprotein having a molecular weight of aproximately 160,000 daltons is also obtained from such cells, of which approximately 90,000 daltons is the unglycosylated moiety and is substantially identical to the unglycosylated moiety of the first glycoprotein. The presence, in a biological specimen, of either of these glycoproteins or of the unglycosylated moiety is indicative of the presence of cells infected by human T-cell leukemia virus. An assay for the glycoprotein or its unglycosylated moiety is a useful diagnostic procedure for determining such infection in biological specimens.

5045448, Sep 3, 1991

Dec 10, 1987

7/131201

Myron E. Essex - Sharon MA
Tun-Hou Lee - Newton MA

President and Fellows of Harvard College - Cambridge MA

G01N 33569, G01N 33535

435 5

A first glycoprotein having a molecular weight of approximately 61,000-68,000 daltons in the MJ, C5-MJ, C91 PL or HUT-102 cell lines, of which 46,000 to 48,000 is the unglycosylated moiety, is obtained from cells infected with human T cell leukemia virus. A second glycoprotein having a molecular weight of approximately 45,000-52,000 daltons is also obtained from such cells and is in large part identical to the NH. sub. 2 -terminal end of the first glycoprotein. The presence, in a biological specimen, of antibody to the antigenic determinant of either of these proteins is indicative of the presence of cells infected by human T cell leukemia virus. An assay for the antibody is a useful diagnostic procedure for determining such infection in biological specimens.

4743678, May 10, 1988

Apr 13, 1984

6/598673

Myron E. Essex - Sharon MA
Tun-Hou Lee - Newton MA

President and Fellows of Harvard College - Cambridge MA

C07K 1504

530350

A first glycoprotein having a molecular weight of approximately 61,000-68,000 daltons in the MJ, C5-MJ, C91 PL or HUT-102 cell lines, of which 46,000 to 48,000 is the unglycosylated moiety, is obtained from cells infected with human T cell leukemia virus. A second glycoprotein having a molecular weight of approximately 45,000-52,000 daltons is also obtained from such cells and is in large part identical to the NH. sub. 2 -terminal end of the first glycoprotein. The presence, in a biological specimen, of antibody to the antigenic determinant of either of these proteins is indicative of the presence of cells infected by human T cell leukemia virus. An assay for the antibody is a useful diagnostic procedure for determining such infection in biologial specimens.

6103238, Aug 15, 2000

Mar 13, 1992

7/850770

Myron E. Essex - Sharon MA
Tun-Hou Lee - Newton MA
Woan-Ruoh Lee - Brookline MA
Chun-Nan Lee - Brookline MA

President and Fellows of Harvard College - Cambridge MA

A61K 3921, A61K 39395, A61K 3942, A61K 3940

4241881

Selective deglycosylation of HIV-1 envelope proteins enhances their ability to elicit a protective immune response in people. Glycosylation can reduce or prevent immunological recognition of envelope protein domains. Selective deglycosylation exposes these domains and improves the opportunity for a protective immune response. Deglycosylation which produces substantial conformational changes (as determined by loss of infectivity) should be avoided. Recombinant HIV-1 envelope glycoproteins are generated which have primary amino acid sequence mutation(s) in consensus sequence(s) for N-linked glycosylation (sugar attachment), so as to prevent glycosylation at that site(s). The position of such genetic deglycosylation is important and should be between the C terminus of gp120 and the Cys at the N-terminal side of the cysteine loop containing the hyper-variable region 3 (V3) (this Cys is generally positioned about at residue 296, counting from the N-terminus of gp120). The mutant glycoprotein should be deglycosylated such that the total molecular mass of the mutant gp120 component is less than 90% (more preferably less than 75%) of the corresponding fully glycosylated wild type gp120 component to maximize a useful immune response.

5731142, Mar 24, 1998

May 17, 1994

8/245077

Myron E. Essex - Sharon MA
Tun-Hou Lee - Newton MA

President and Fellows of Harvard College - Cambridge MA

C12Q 170, G01N 33564, C07K 1416

435 5

A first glycoprotein having a molecular weight of approximately 120,000 daltons in the H9/HTLV-III cell line, of which approximately 90,000 daltons is the unglycosylated moiety, is obtained from cells infected with human T-cell leukemia virus, type III. A second glycoprotein having a molecular weight of approximately 160,000 daltons is also obtained from such cells, of which approximately 90,000 daltons is the unglycosylated moiety and is substantially identical to the unglycosylated moiety of the first glycoprotein. The presence, in a biological specimen, of either of these unglycosylated or of the unglycosylated moiety is indicative of the presence of cells infected by human T-cell leukemia virus. An assay for the glycoprotein or its unglycosylated moiety is a useful diagnostic procedure for determining such infection in biological specimens.

5707864, Jan 13, 1998

Nov 23, 1992

7/979966

Myron E. Essex - Sharon MA
Xiaofang Yu - Columbia MD
Tun-Hou Lee - Newton MA

President and Fellows of Harvard College - Cambridge MA

C12N 1549, C12N 510, C12N 1563, C07K 14155

435325

Nucleic acid constructs encoding mutated human immunodeficiency virus matrix proteins are described. The mutated proteins lower the incorporation of envelope polypeptides in viral particles, disrupt viral assembly or disrupt viral entry into uninfected cells.

5068174, Nov 26, 1991

Oct 25, 1988

7/250309

Myron E. Essex - Sharon MA
Jonathan S. Allan - Westwood MA
Tun-Hou Lee - Newton MA

President and Fellows of Harvard College - Cambridge MA

G01N 33569

435 5

Cells infected with HTLV-III yield a protein (p27) having an apparent molecular weight of about 27,000 daltons. This invention was made in the course of work for the NIH under grants CA37466, CA23885, and CA2T32-CA09031, and the United States Government has certain rights in the invention.

5736391, Apr 7, 1998

Jun 6, 1995

8/467933

Myron E. Essex - Sharon MA
Xiaofang Yu - Jamaica Plain MA
Tun-Hou Lee - Newton MA

President and Fellows of Harvard College - Cambridge MA

C12N 1549, C12N 1579, C07H 2104, A61K 4800

4353201

Nucleic acid constructs encoding mutated human immunodeficiency virus gp41 polypeptides are described. The mutated polypeptides are effective to disrupt viral replication of HIV or disrupt the assembly of viral Env proteins in an HIV infected cell.