Abstract
A putative zinc protease gene operon from Ehrlichia canis was cloned and sequenced. A genomic library was constructed in a pHG165 plasmid vector using Sau3A partially digested E. canis chromosomal DNA. Sequence analysis of the insert DNA from this clone indicated two open reading frames with a size of 1314 and 1350bp that encodes for ProA and ProB, respectively. Based on BLAST analyses, ProA and ProB share 20-30% identities with members of the eukaryotic mitochondrial processing peptidase (MPP) subfamily, which are heterodimers containing α and β subunits. The subunits share a 20% of identity, but only MPP-β contains a conserved zincbinding motif, His-Xaa-Xaa-Glu-His (HXXEH). proA and proB are also detectable in E. canis and Ehrlichia chaffeensis, but not the Anaplasma phagocytophila. 5′-RACE revealed that the 5′ end of the proA mRNA is heterogeneous, containing additional adenine residues that may be directed by pseudo-templated transcription. Although ProA was identified in both E. canis and E. chaffeensis, ProB was detected only in E. canis. ProA and ProB were both detectable in E. canis-infected DH82 cells. Sera from dogs, which were either naturally or experimentally infected with E. canis, recognized both the recombinant protein antigens.
| Original language | English |
|---|---|
| Pages (from-to) | 109-121 |
| Number of pages | 13 |
| Journal | DNA Sequence - Journal of DNA Sequencing and Mapping |
| Volume | 14 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2003 Apr 1 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Genetics
- Endocrinology
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Cloning and characterization of putative zinc protease genes of Ehrlichia canis. / Teng, Ching Hao; Barr, Stephen C.; Chang, Yung Fu.
In: DNA Sequence - Journal of DNA Sequencing and Mapping, Vol. 14, No. 2, 01.04.2003, p. 109-121.Research output: Contribution to journal › Article
TY - JOUR
T1 - Cloning and characterization of putative zinc protease genes of Ehrlichia canis
AU - Teng, Ching Hao
AU - Barr, Stephen C.
AU - Chang, Yung Fu
PY - 2003/4/1
Y1 - 2003/4/1
N2 - A putative zinc protease gene operon from Ehrlichia canis was cloned and sequenced. A genomic library was constructed in a pHG165 plasmid vector using Sau3A partially digested E. canis chromosomal DNA. Sequence analysis of the insert DNA from this clone indicated two open reading frames with a size of 1314 and 1350bp that encodes for ProA and ProB, respectively. Based on BLAST analyses, ProA and ProB share 20-30% identities with members of the eukaryotic mitochondrial processing peptidase (MPP) subfamily, which are heterodimers containing α and β subunits. The subunits share a 20% of identity, but only MPP-β contains a conserved zincbinding motif, His-Xaa-Xaa-Glu-His (HXXEH). proA and proB are also detectable in E. canis and Ehrlichia chaffeensis, but not the Anaplasma phagocytophila. 5′-RACE revealed that the 5′ end of the proA mRNA is heterogeneous, containing additional adenine residues that may be directed by pseudo-templated transcription. Although ProA was identified in both E. canis and E. chaffeensis, ProB was detected only in E. canis. ProA and ProB were both detectable in E. canis-infected DH82 cells. Sera from dogs, which were either naturally or experimentally infected with E. canis, recognized both the recombinant protein antigens.
AB - A putative zinc protease gene operon from Ehrlichia canis was cloned and sequenced. A genomic library was constructed in a pHG165 plasmid vector using Sau3A partially digested E. canis chromosomal DNA. Sequence analysis of the insert DNA from this clone indicated two open reading frames with a size of 1314 and 1350bp that encodes for ProA and ProB, respectively. Based on BLAST analyses, ProA and ProB share 20-30% identities with members of the eukaryotic mitochondrial processing peptidase (MPP) subfamily, which are heterodimers containing α and β subunits. The subunits share a 20% of identity, but only MPP-β contains a conserved zincbinding motif, His-Xaa-Xaa-Glu-His (HXXEH). proA and proB are also detectable in E. canis and Ehrlichia chaffeensis, but not the Anaplasma phagocytophila. 5′-RACE revealed that the 5′ end of the proA mRNA is heterogeneous, containing additional adenine residues that may be directed by pseudo-templated transcription. Although ProA was identified in both E. canis and E. chaffeensis, ProB was detected only in E. canis. ProA and ProB were both detectable in E. canis-infected DH82 cells. Sera from dogs, which were either naturally or experimentally infected with E. canis, recognized both the recombinant protein antigens.
UR - http://www.scopus.com/inward/record.url?scp=0037382852&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037382852&partnerID=8YFLogxK
U2 - 10.1080/1042517031000073736
DO - 10.1080/1042517031000073736
M3 - Article
C2 - 12825352
AN - SCOPUS:0037382852
VL - 14
SP - 109
EP - 121
JO - DNA Sequence - Journal of DNA Sequencing and Mapping
JF - DNA Sequence - Journal of DNA Sequencing and Mapping
SN - 1042-5179
IS - 2
ER -