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J E Coligan

Publications and source records attributed to J E Coligan.

At least 235 records · Page 13Linked to original sources
PubMed1981

Primary structure of murine major histocompatibility complex alloantigens. Amino acid sequence of the NH2-terminal ninety-eight residues of the H-2Db glycoprotein.

The NH2-terminal 98 amino acid residues of the murine histocompatibility antigen H-2Db have been assigned using radiochemical methodology. This represents the first extensive, continuous sequence information for a histocompatibility antigen encoded by the H-2D locus and allows comparison with the recently determined amino acid sequence of the H-2Kb molecule. The amino acid sequence was obtained from the sequences of three CNBr peptides, CN-E, CN-D, and CN-B, which comprise residues 1-5, 6-52, and 53-98, respectively. The amino acid sequence of CN-E was determined directly while the sequences of CN-D and CN-B were determined by NH2-terminal sequence analyses and sequence determinations of peptides produced by thrombin, staphylococcal V8 protease, and trypsin cleavage. Alignment of the CNBr peptides was accomplished by NH2-terminal sequence analysis of the H-2Db papain fragment (CN-E to CN-D) and by analyzing peptides from a tryptic digest of the intact H-2Db molecule. Positive identification was possible for all amino acids except Asp and Asn-86 which were indirectly assigned (in italics). The sequence obtained was Gly-Pro-His-Ser-Met-Arg-Tyr-Phe-Glu-Thr-Ala-Val-Ser-Arg-Pro-Gly-Leu-Glu-Glu-Pro -Arg-Tyr-Ile-Ser-Val-Gly-Tyr-Val-Asp-Asn-Lys-Glu-Phe-Val-Arg-Phe-Asp-Ser-Asp-Ala-Glu-Asn-Pro-Arg-Tyr-Glu-Pro-Arg-Ala-Pro-Trp-Met-Glu-Gln-Glu-Gly-Pro-Glu-Tyr-T rp-Glu-Arg-Glu-Thr-Gln-Lys-Ala-Lys-Gly-Gln-Glu-Gln-Trp-Phe-Arg-Val-Ser-Leu-Arg-Asn-Leu-Leu-Gly-Tyr-Tyr-Asn-Gln-Ser-Ala-Gly-Gly-Ser-His-Thr-Leu-Gln-Gln-Met.

Amino Acid Sequence↗
PubMed1981

Complete amino acid sequence of murine beta 2-microglobulin: structural evidence for strain-related polymorphism.

Primary structural analyses of beta 3-microglobulin isolated from the tumor cell lines EL4.BU (derived from a C57BL/6 mouse) and C14 (derived from a BALB/c mouse) have revealed the presence of an amino acid difference at position 85 of this molecule. beta 2-Microglobulin isolated from histocompatibility antigens of EL4.BU has alanine at this position, whereas that from C14 has aspartic acid. Determination of the sequence of these molecules has employed radiochemical methodology that was developed in studies of murine histocompatibility antigens. The sequence obtained in this study is: Ile - Gln - Lys - Thr - Pro - Gln - Ile - Gln - Val - Tyr - Ser - Arg - His - Pro - Pro - Glu - Asn - Gly - Lys - Pro - Asn - Ile - Leu - Asn - Cys - Tyr - Val - Thr - Gln - Phe - His - Pro - Pro - His - Ile - Glu - Ile - Gln - Met - Leu - Lys - Asn - Gly - Lys - Lys - Ile Pro - Lys - Val - Glu - Met - Ser - Asp - Met - Ser - Phe - Ser - Lys - Asp - Trp - Ser - Phe - Tyr - Ile - Leu - Ala - His - Thr - Glu - Phe - Thr - Pro - Thr - Glu - Thr - Asp - Thr - Tyr - Ala - Cys - Arg - Val - Lys - His - Ala/Asp - Ser - Met - Ala - Glu - Pro - Lys - Thr - Val - Tyr - Trp - Asp - Arg - Asp - Met. Comparison of the sequence of murine beta 2-microglobulin to the sequences reported for the homologues from man, rabbit, and guinea pig indicate identities of 68%, 66%, and 61%, respectively.

Amino Acid Sequence↗
PubMed1981

Carbohydrate fingerprints of streptococcal cells.

The carbohydrates of whole cells of group A, B, C, D, F, and G streptococci were analyzed with a highly sensitive gas chromatographic procedure. Characteristic chromatographic fingerprints were obtained for each group of streptococci grown in broth cultures or as single colonies on a blood agar plate. Rhamnose, glucose, and N-acetylglucosamine were major components of all the groups. Groups A, C, and F contained very little galactose, and groups A and B showed almost a complete absence of N-acetylgalactosamine. Chromatograms obtained for group B streptococci were distinguished by the presence of 1,4-anhydroglucitol.

Acetylglucosamine↗
PubMed1981

Immunochemical evidence in two haplotypes for at least three D region-encoded molecules, D, L, and R.

Sequential immunoprecipitation analyses have defined a new transplantation antigen, designated R, which in addition to the 2 previously isolated D and L molecules is encoded in the D region. All 3 of these gene products are 45,000 m.w. glycoprotein, and each bears a unique combination of specificities as recognized by monoclonal and/or conventional anti-H-2 sera. Three D region products, D, L, and R, have now been isolated from soluble antigens of both the H-2d and H-2q haplotypes. The resulted reported here also indicate that the loss-mutant BALB/c-H-2dm2 fails to express both Ld and Rd antigens. Further chemical comparisons of the primary structure of R molecules with D and L molecules will now be necessary to determine whether R antigens are the products of a unique gene, as opposed to a glycosylation or conformational variant of D and/or L molecules. In either case, the discovery of 3 D region-encoded gene products in certain haplotypes raises new questions about the evolution and regulation of expression of H-2 loci.

Animals↗
PubMed1980

Primary structure of murine major histocompatibility alloantigens: amino acid sequence of the cyanogen bromide fragment Ia (positions 139-228) from the H-2Kb molecule.

The complete amino acid sequence of the cyanogen bromide (CNBr) fragment Ia (CN-Ia) from the murine histocompatibility antigen H-2Kb has been obtained by using radiosequence methodology. This glycopeptide is the largest CNBr cleavage product of the H-2K molecule and extends from position 139 to position 228. The sequence determined for CN-Ia was Ala-Ala-Leu-Ile-Thr-Lys-His-Lys-Trp-Glu-Gln-Ala-Gly-Glu-Ala-Glu-Arg-Leu-Arg-Ala -Tyr-Leu-Glu-Gly-Thr-Cys-Val-Glu-Trp-Leu-Arg-Arg-Tyr-Leu-Lys-Ans-Gly-(Asn)-Ala- Thr-Leu-Leu-Arg-Thr-Asp-Ser-Pro-Lys-Ala-His-Val-Thr-His-His-Ser-Arg-Pro-Asp-Asp -Lys-Val-Thr-Leu-Arg-Cys-Trp-Ala-Leu-Gly-Phe-Tyr-Pro-Ala-Asp-Ile-Thr-Leu-Thr-Tr p-Gln-Leu-Asn-Gly-Glu-Glu-Leu-Ile-Gln-Aps-Met. The data were obtained by analysis of fragments derived by thrombic, tryptic, chymotryptic, and V8 protease digestion of CN-Ia. A carbohydrate moiety is attached to Asn at position 176. Homology between this 90 amino acid stretch of H-2Kb and HLA-B7 [Orr, H. T., Lopez de Castro, J. A., Lancer, D., & Strominger, J. L. (1979) Biochemistry 18, 5711] is 68%, and differences are noted at positions 176, 177, and 178 which in the H-2 molecule are the attachment region for a second carbohydrate moiety. No carbohydrate was detected in this position for HLA-B7 [Orr, H. T. Lopez de Castro, J. A. Lancet, D., & Strominger, J. L. (1979) Biochemistry 18, 5711].

Amino Acid Sequence↗
PubMed1980

Primary structure of murine major histocompatibility complex alloantigens: completion of the sequence of the amino-terminal 284 residues of H-2Kb.

The primary structure of the COOH-terminal cyanogen bromide (CNBr) cleavage fragment Ic (CN-Ic) of the extracellular portion of the murine histocompatibility antigen H-2Kb has been completed. CN-Ic contains a site of papain cleavage which has been utilized for solubilizing H-2Kb by cleaving off the membrane integrating portion of the molecule. The amino acid sequence of CN-Ic has been determined by using peptides recovered after trypsin digestion of CN-Ic before and after blockage of lysine groups with citraconic anhydride. Overlapping sequences for the tryptic fragments were obtained by amino-terminal sequence analysis. The sequence of fragment CN-Ic, which spans residues 229-284 in H-2Kb, is as follows: Glu-Leu-Val-Glu-Thr-Arg-Pro-Ala-Gly-Asp-Gly-Thr-Phe-Gln-Lys-Trp-Ala-Ser-Val-Val-Pro-Leu-Gly-Lys-Glu-Gln-Tyr-Tyr-Thr-Cys-His-Val-Tyr-Gln-Gln-Gly-Leu-Pro-Gln-Pro-Leu-Thr-Leu-Arg-Trp-Asp-Glu-Pro-Pro-Ser-Thr-Val-Ser-Asn-Met. This amino acid sequence determination completes the primary structure of the amino terminal 284 residues of H-2Kb, that portion of this histocompatibility antigen which is external to the cell membrane and which contains antigenic determinants. It was also possible to identify Val-281 as a papain cleavage site within CN-Ic. The completed structure was analyzed solely by radiochemical methods. The structure obtained for H-2Kb is 71% homologous to the reported structure of HLA-B7, a human homologue.

Amino Acid Sequence↗
PubMed1980

Primary structure of murine major histocompatibility complex alloantigens: amino acid sequence of the amino-terminal one hundred and seventy-three residues of the H-2Kb glycoprotein.

The amino-terminal 173 residues of the murine histocompatibility antigen H-2Kb have been assigned by using radiochemical methodology. The complete sequence of an 86 residue glycopeptide (CN-Ib), which is one of the five major CNBr fragments of Kb, was determined by analysis of peptides obtained from digests using thrombin and V8 staphylococcal protease. Complete sequences were obtained for the three large thrombic peptides, and these were aligned by using peptides from the V8 protease digest. Alignment of the CNBr fragments was carried out by using [35S]Met-labeled peptides from a tryptic digest of the papain-cleaved H-2Kb molecule. Positive identification was possible for all the common amino acids except Asp (Asp) which was indirectly assigned and which is designated in italics. The sequence obtained in our studies was Gly-Pro-His-Ser-Leu-Arg-Tyr-Phe-Val-Thr-Ala-Val-Ser-Arg-Pro-Gly-Leu-Gly-Glu-Pro-Arg-Tyr-Met-Glu-Val-Gly-Tyr-Val-Asp-Asp-Thr-Glu-Phe-Val-Arg-Phe-Asp-Ser-Asp-Ala-Glu-Asn-Pro-Arg-Tyr-Glu-Pro-Arg-Ala-Arg-Trp-Met-Glu-Gln-Glu-Gly-Pro-Glu-Tyr-Trp-Glu-Arg-Glu-Thr-Gln-Lys-Ala-Lys-Gly-Asn-Glu-Gln-Ser-Phe-Arg-Val-Asp-Leu-Arg-Thr-Leu-Leu-Gly-Tyr-Tyr-(Asn)-Gln-Ser-Lys-Gly-Gly-Ser-His-Thr-Ile-Gln-Val-Ile-Ser-Gly-Cys-Glu-Val-Gly-Ser-Asp-Gly-Arg-Leu-Leu-Arg-Gly-Tyr-Gln-Gln-Tyr-Ala-Tyr-Asp-Gly-Cys-Asp-Tyr-Ile-Ala-Leu-Asn-Glu-Asp-Leu-Lys-Thr-Trp-Thr-Ala-Ala-Asp-Met-Ala-Ala-Leu-Ile-Thr-Lys-His-Lys-Trp-Glu-Gln-Ala-Gly-Glu-Ala-Glu-Arg-Leu-Arg-Ala-Tyr-Leu-Glu-Gly-Thr-Cys-Val-Glu-Trp-Leu-Arg-Arg-Tyr-Leu-Lys. These data represent the longest reported amino acid sequence determined by utilizing radiochemical methodology and provide the first extensive information on the primary structure of murine histocompatibility antigens.

Amino Acid Sequence↗
PubMed1980

Isolation, characterization and amino acid sequence studies of the cyanogen bromide fragments of the H-2Dd glycoprotein.

The papain-solubilized fragment of the H-2Dd antigen, representing the NH2-terminal 80% of the native glycoprotein, can be fragmented into five polypeptides using CNBr cleavage. These fragments have been isolated, characterized and subjected to amino acid sequence analysis using radiochemical microtechniques. It was possible to align these CNBr fragments by comparison of their NH2-terminal amino acid sequence with the known amino acid sequence of the H-2Kb molecule. Thus, the NH2-terminal fragment, D, contains 23 residues and is followed by a glycopeptide, fragment C, of 75 residues. Following fragment C are three fragments held together by disulfide bonds: fragment b4, which has 40 amino acid residues, a second glycopeptide, fragment b2, of 90 residues, and fragment b3, a peptide of approximately 55 residues which terminates at the site of papain cleavage. The complete amino acid sequence of the NH2-terminal CNBr fragment, D, has been determined, and this is presented here along with sequence data for the NH2-terminal 30 residues of each of the other four CNBr fragments of the papain fragment of H-2Dd. A total of 146 positions have been examined in the approximately 280-residue H-2Ddpapain molecule, and a total of 127 residues have been positively determined. Most of the unassigned positions may be tentatively assigned as Asp or Asn, the only amino acids so far not incorporated in radiolabeled form by our metabolic labeling procedures into the H-2Dd molecule. Comparison of the sequence data obtained for the H-2Dd molecule to data available for other histocompatibility antigens revealed homologies of approximately 90% with H-2Kb and H-2Ld, and approximately 75% with HLA-B7 and HLA-A2.

Amino Acid Sequence↗
PubMed1980

Comparison of alloantisera and hybridoma antibody for purification of the H-2Db murine histocompatibility antigen and preliminary molecular characterization of this antigen.

Previous studies on the determination of the complete amino acid sequence of H-2 molecules have relied on alloantisera to purify the H-2 molecules by immunoprecipitation. In this study, directed toward the determination of the complete amino acid sequence of the H-2Db molecule, it was found that all H-2.2 alloantisera examined had very low antibody titers when analyzed by immunoprecipitation and that most of these antisera reacted with not only the H-2Db heavy chain but also with a 75,000 dalton virus-associated glycoprotein (gp 75). The problems encountered with conventional alloantisera were surmounted by utilizing a monoclonal antibody from hybridoma B22-249R1 obtained as described by Hämmerling et al. (1979) and maintained in ascites form in (CBA x Balb/c) F1 mice. This antibody reacted with only 45,000 molecular weight material and had the added advantage of requiring only 0.1 ml of hybridoma ascites fluid to bind all of the H-2Db antigen from 3 x 10(8) EK-4 tumor cells. Biochemical examination of the purified H-2Db molecule showed that it possessed overall structural properties similar to other previously characterized H-2 molecules. An NH2-terminal amino acid sequence was determined for the H-2Db molecule for 28 residues and this sequence was compared to the complete NH2-terminal sequences of the H-2Kb and H-2Dd molecules, and the partial NH2-terminal sequence for the H-2Ld molecule; these comparisons indicated 82%, 75% and 100% homology respectively. In addition, these preliminary studies indicated that there was little or no beta-2-microglobulin (beta 2 mu) in the immunoprecipitates with the H2-2Db heavy chain. This lack of beta 2 mu in the immunoprecipitates was found to be true for alloantisera directed against private or public specificities, a xenoantiserum (sheep anti-H-2b), or hybridoma antibody used in the immunoprecipitation.

Amino Acid Sequence↗
PubMed1980

Primary structural studies of an H-2L molecule confirm that it is a unique gene product with homology to H-2K and H-2D antigens.

Radiochemical methodology has been used in the isolation and preliminary biochemical characterization of the murine H-2Ld major histocompatibility complex gene product. The radiolabeled molecule was isolated by immunoprecipitation from the glycoprotein fraction of detergent-solubilized H-2d tumor cells. Six major CNBr fragments were isolated from a papain fragment of this molecule; three of the fragments are connected by disulfide bonds. Due to the high degree of homology between major transplantation antigens, it was possible to align the fragments by comparison of their amino acid sequences to that of the H-2Kb gene product. Of the positions available for comparison between H-2Ld and H-2Kb, H-2Dd, and H-2Kd gene products, 61 out of 80 (78%), 45 out of 55 (82%), and 12 out of 15 (80%), respectively, are identical. Differences between the Ld and Kb and Dd molecules are distributed throughout the amino acid sequence. These data indicate that the H-2Ld gene product is a molecular species distinct from, but homologous to, the H-2K and H-2D gene products.

Amino Acid Sequence↗