Cloning and sequence analysis of bovine corneal antigen (coag) cdna

identification of host-parasite protein calgranulin c

John D Gottsch, S. H. Liu

Research output: Contribution to journalArticle

Abstract

Purpose. A cornea-associated antigen (CO-Ag) has been implicated in the pathogenesis of Mooren's ulcer. The study design was to isolate a full-length clone encoding CO-Ag from a bovine corneal cDNA library so that a complete sequence analysis might further define the possible role of this protein in Mooren's ulcer. Methods. A DNA fragment of CO-Ag was generated using unique oligonucleotide primers and reverse transcription polymerase chain reaction. This fragment was used as a probe to obtain cDNA clones from a bovine corneal cDNA library. Results. The cDNA insert sequence was 273 nucleotides in length for the entire mRNA coding region, 212 nucleotides in the 5' untranslated region, 83 nucleotides in the 3' untranslated region and a poly(A) tail. The DNA base sequence of this clone also contained a standard initiation codon, termination codon, and the polyadenylation signal. This cDNA predicts a protein which contains 91 amino acids with a molecular weight of 10,584 daltons. The cDNA and deduced amino acid sequence of CO-Ag are completely identical to a S-100 protein, bovine calgranulin C, whose human counterpart has been isolated from neutrophils and has been isolated on the surface of filarial nematodes. Conclusions. We report the isolation and analysis of a cDNA clone containing the complete coding sequence of the CO-Ag protein, the protein identification by deduced amino acid sequence, and the possible relationship of CO-Ag in a hostparasite interaction in the etiology of Mooren's ulcer.

Original languageEnglish (US)
JournalInvestigative Ophthalmology and Visual Science
Volume38
Issue number4
StatePublished - 1997

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Leukocyte L1 Antigen Complex
Cornea
Sequence Analysis
Organism Cloning
Parasites
Antigens
Complementary DNA
Clone Cells
Ulcer
Proteins
Nucleotides
Gene Library
Amino Acid Sequence
Messenger RNA
Polyadenylation
DNA Primers
Initiator Codon
S100 Proteins
Terminator Codon
5' Untranslated Regions

ASJC Scopus subject areas

  • Ophthalmology

Cite this

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title = "Cloning and sequence analysis of bovine corneal antigen (coag) cdna: identification of host-parasite protein calgranulin c",
abstract = "Purpose. A cornea-associated antigen (CO-Ag) has been implicated in the pathogenesis of Mooren's ulcer. The study design was to isolate a full-length clone encoding CO-Ag from a bovine corneal cDNA library so that a complete sequence analysis might further define the possible role of this protein in Mooren's ulcer. Methods. A DNA fragment of CO-Ag was generated using unique oligonucleotide primers and reverse transcription polymerase chain reaction. This fragment was used as a probe to obtain cDNA clones from a bovine corneal cDNA library. Results. The cDNA insert sequence was 273 nucleotides in length for the entire mRNA coding region, 212 nucleotides in the 5' untranslated region, 83 nucleotides in the 3' untranslated region and a poly(A) tail. The DNA base sequence of this clone also contained a standard initiation codon, termination codon, and the polyadenylation signal. This cDNA predicts a protein which contains 91 amino acids with a molecular weight of 10,584 daltons. The cDNA and deduced amino acid sequence of CO-Ag are completely identical to a S-100 protein, bovine calgranulin C, whose human counterpart has been isolated from neutrophils and has been isolated on the surface of filarial nematodes. Conclusions. We report the isolation and analysis of a cDNA clone containing the complete coding sequence of the CO-Ag protein, the protein identification by deduced amino acid sequence, and the possible relationship of CO-Ag in a hostparasite interaction in the etiology of Mooren's ulcer.",
author = "Gottsch, {John D} and Liu, {S. H.}",
year = "1997",
language = "English (US)",
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journal = "Investigative Ophthalmology and Visual Science",
issn = "0146-0404",
publisher = "Association for Research in Vision and Ophthalmology Inc.",
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T2 - identification of host-parasite protein calgranulin c

AU - Gottsch, John D

AU - Liu, S. H.

PY - 1997

Y1 - 1997

N2 - Purpose. A cornea-associated antigen (CO-Ag) has been implicated in the pathogenesis of Mooren's ulcer. The study design was to isolate a full-length clone encoding CO-Ag from a bovine corneal cDNA library so that a complete sequence analysis might further define the possible role of this protein in Mooren's ulcer. Methods. A DNA fragment of CO-Ag was generated using unique oligonucleotide primers and reverse transcription polymerase chain reaction. This fragment was used as a probe to obtain cDNA clones from a bovine corneal cDNA library. Results. The cDNA insert sequence was 273 nucleotides in length for the entire mRNA coding region, 212 nucleotides in the 5' untranslated region, 83 nucleotides in the 3' untranslated region and a poly(A) tail. The DNA base sequence of this clone also contained a standard initiation codon, termination codon, and the polyadenylation signal. This cDNA predicts a protein which contains 91 amino acids with a molecular weight of 10,584 daltons. The cDNA and deduced amino acid sequence of CO-Ag are completely identical to a S-100 protein, bovine calgranulin C, whose human counterpart has been isolated from neutrophils and has been isolated on the surface of filarial nematodes. Conclusions. We report the isolation and analysis of a cDNA clone containing the complete coding sequence of the CO-Ag protein, the protein identification by deduced amino acid sequence, and the possible relationship of CO-Ag in a hostparasite interaction in the etiology of Mooren's ulcer.

AB - Purpose. A cornea-associated antigen (CO-Ag) has been implicated in the pathogenesis of Mooren's ulcer. The study design was to isolate a full-length clone encoding CO-Ag from a bovine corneal cDNA library so that a complete sequence analysis might further define the possible role of this protein in Mooren's ulcer. Methods. A DNA fragment of CO-Ag was generated using unique oligonucleotide primers and reverse transcription polymerase chain reaction. This fragment was used as a probe to obtain cDNA clones from a bovine corneal cDNA library. Results. The cDNA insert sequence was 273 nucleotides in length for the entire mRNA coding region, 212 nucleotides in the 5' untranslated region, 83 nucleotides in the 3' untranslated region and a poly(A) tail. The DNA base sequence of this clone also contained a standard initiation codon, termination codon, and the polyadenylation signal. This cDNA predicts a protein which contains 91 amino acids with a molecular weight of 10,584 daltons. The cDNA and deduced amino acid sequence of CO-Ag are completely identical to a S-100 protein, bovine calgranulin C, whose human counterpart has been isolated from neutrophils and has been isolated on the surface of filarial nematodes. Conclusions. We report the isolation and analysis of a cDNA clone containing the complete coding sequence of the CO-Ag protein, the protein identification by deduced amino acid sequence, and the possible relationship of CO-Ag in a hostparasite interaction in the etiology of Mooren's ulcer.

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