Eimeria maxima phosphatidylinositol 4-phosphate 5-kinase

Locus sequencing, characterization, and cross-phylum comparison

Mei Yen Goh, Mei Zhen Pan, Damer P. Blake, Kiew Lian Wan, Beng Kah Song

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Phosphatidylinositol 4-phosphate 5-kinase (PIP5K) may play an important role in host-cell invasion by the Eimeria species, protozoan parasites which can cause severe intestinal disease in livestock. Here, we report the structural organization of the PIP5K gene in Eimeria maxima (Weybridge strain). Two E. maxima BAC clones carrying the E. maxima PIP5K (EmPIP5K) coding sequences were selected for shotgun sequencing, yielding a 9.1-kb genomic segment. The EmPIP5K coding region was initially identified using in silico gene-prediction approaches and subsequently confirmed by mapping rapid amplification of cDNA ends and RT-PCR-generated cDNA sequence to its genomic segment. The putative EmPIP5K gene was located at position 710-8036 nt on the complimentary strand and comprised of 23 exons. Alignment of the 1147 amino acid sequence with previously annotated PIP5K proteins from other Apicomplexa species detected three conserved motifs encompassing the kinase core domain, which has been shown by previous protein deletion studies to be necessary for PIP5K protein function. Phylogenetic analysis provided further evidence that the putative EmPIP5K protein is orthologous to that of other Apicomplexa. Subsequent comparative gene structure characterization revealed events of intron loss/gain throughout the evolution of the apicomplexan PIP5K gene. Further scrutiny of the genomic structure revealed a possible trend towards "intron gain" between two of the motif regions. Our findings offer preliminary insights into the structural variations that have occurred during the evolution of the PIP5K locus and may aid in understanding the functional role of this gene in the cellular biology of apicomplexan parasites.

Original languageEnglish
Pages (from-to)611-620
Number of pages10
JournalParasitology Research
Volume108
Issue number3
DOIs
Publication statusPublished - Mar 2011

Fingerprint

Eimeria maxima
Eimeria
phosphatidylinositols
phosphotransferases (kinases)
phosphates
loci
Apicomplexa
Genes
genes
genomics
protein kinases
Introns
introns
Parasites
Proteins
Complementary DNA
parasites
Intestinal Diseases
cell invasion
rapid amplification of cDNA ends

ASJC Scopus subject areas

  • Parasitology
  • Infectious Diseases

Cite this

Eimeria maxima phosphatidylinositol 4-phosphate 5-kinase : Locus sequencing, characterization, and cross-phylum comparison. / Goh, Mei Yen; Pan, Mei Zhen; Blake, Damer P.; Wan, Kiew Lian; Song, Beng Kah.

In: Parasitology Research, Vol. 108, No. 3, 03.2011, p. 611-620.

Research output: Contribution to journalArticle

Goh, Mei Yen ; Pan, Mei Zhen ; Blake, Damer P. ; Wan, Kiew Lian ; Song, Beng Kah. / Eimeria maxima phosphatidylinositol 4-phosphate 5-kinase : Locus sequencing, characterization, and cross-phylum comparison. In: Parasitology Research. 2011 ; Vol. 108, No. 3. pp. 611-620.
@article{8ab7c076524141899fd8664bbc6ebff9,
title = "Eimeria maxima phosphatidylinositol 4-phosphate 5-kinase: Locus sequencing, characterization, and cross-phylum comparison",
abstract = "Phosphatidylinositol 4-phosphate 5-kinase (PIP5K) may play an important role in host-cell invasion by the Eimeria species, protozoan parasites which can cause severe intestinal disease in livestock. Here, we report the structural organization of the PIP5K gene in Eimeria maxima (Weybridge strain). Two E. maxima BAC clones carrying the E. maxima PIP5K (EmPIP5K) coding sequences were selected for shotgun sequencing, yielding a 9.1-kb genomic segment. The EmPIP5K coding region was initially identified using in silico gene-prediction approaches and subsequently confirmed by mapping rapid amplification of cDNA ends and RT-PCR-generated cDNA sequence to its genomic segment. The putative EmPIP5K gene was located at position 710-8036 nt on the complimentary strand and comprised of 23 exons. Alignment of the 1147 amino acid sequence with previously annotated PIP5K proteins from other Apicomplexa species detected three conserved motifs encompassing the kinase core domain, which has been shown by previous protein deletion studies to be necessary for PIP5K protein function. Phylogenetic analysis provided further evidence that the putative EmPIP5K protein is orthologous to that of other Apicomplexa. Subsequent comparative gene structure characterization revealed events of intron loss/gain throughout the evolution of the apicomplexan PIP5K gene. Further scrutiny of the genomic structure revealed a possible trend towards {"}intron gain{"} between two of the motif regions. Our findings offer preliminary insights into the structural variations that have occurred during the evolution of the PIP5K locus and may aid in understanding the functional role of this gene in the cellular biology of apicomplexan parasites.",
author = "Goh, {Mei Yen} and Pan, {Mei Zhen} and Blake, {Damer P.} and Wan, {Kiew Lian} and Song, {Beng Kah}",
year = "2011",
month = "3",
doi = "10.1007/s00436-010-2104-7",
language = "English",
volume = "108",
pages = "611--620",
journal = "Zeitschrift fur Parasitenkunde",
issn = "0932-0113",
publisher = "Springer Verlag",
number = "3",

}

TY - JOUR

T1 - Eimeria maxima phosphatidylinositol 4-phosphate 5-kinase

T2 - Locus sequencing, characterization, and cross-phylum comparison

AU - Goh, Mei Yen

AU - Pan, Mei Zhen

AU - Blake, Damer P.

AU - Wan, Kiew Lian

AU - Song, Beng Kah

PY - 2011/3

Y1 - 2011/3

N2 - Phosphatidylinositol 4-phosphate 5-kinase (PIP5K) may play an important role in host-cell invasion by the Eimeria species, protozoan parasites which can cause severe intestinal disease in livestock. Here, we report the structural organization of the PIP5K gene in Eimeria maxima (Weybridge strain). Two E. maxima BAC clones carrying the E. maxima PIP5K (EmPIP5K) coding sequences were selected for shotgun sequencing, yielding a 9.1-kb genomic segment. The EmPIP5K coding region was initially identified using in silico gene-prediction approaches and subsequently confirmed by mapping rapid amplification of cDNA ends and RT-PCR-generated cDNA sequence to its genomic segment. The putative EmPIP5K gene was located at position 710-8036 nt on the complimentary strand and comprised of 23 exons. Alignment of the 1147 amino acid sequence with previously annotated PIP5K proteins from other Apicomplexa species detected three conserved motifs encompassing the kinase core domain, which has been shown by previous protein deletion studies to be necessary for PIP5K protein function. Phylogenetic analysis provided further evidence that the putative EmPIP5K protein is orthologous to that of other Apicomplexa. Subsequent comparative gene structure characterization revealed events of intron loss/gain throughout the evolution of the apicomplexan PIP5K gene. Further scrutiny of the genomic structure revealed a possible trend towards "intron gain" between two of the motif regions. Our findings offer preliminary insights into the structural variations that have occurred during the evolution of the PIP5K locus and may aid in understanding the functional role of this gene in the cellular biology of apicomplexan parasites.

AB - Phosphatidylinositol 4-phosphate 5-kinase (PIP5K) may play an important role in host-cell invasion by the Eimeria species, protozoan parasites which can cause severe intestinal disease in livestock. Here, we report the structural organization of the PIP5K gene in Eimeria maxima (Weybridge strain). Two E. maxima BAC clones carrying the E. maxima PIP5K (EmPIP5K) coding sequences were selected for shotgun sequencing, yielding a 9.1-kb genomic segment. The EmPIP5K coding region was initially identified using in silico gene-prediction approaches and subsequently confirmed by mapping rapid amplification of cDNA ends and RT-PCR-generated cDNA sequence to its genomic segment. The putative EmPIP5K gene was located at position 710-8036 nt on the complimentary strand and comprised of 23 exons. Alignment of the 1147 amino acid sequence with previously annotated PIP5K proteins from other Apicomplexa species detected three conserved motifs encompassing the kinase core domain, which has been shown by previous protein deletion studies to be necessary for PIP5K protein function. Phylogenetic analysis provided further evidence that the putative EmPIP5K protein is orthologous to that of other Apicomplexa. Subsequent comparative gene structure characterization revealed events of intron loss/gain throughout the evolution of the apicomplexan PIP5K gene. Further scrutiny of the genomic structure revealed a possible trend towards "intron gain" between two of the motif regions. Our findings offer preliminary insights into the structural variations that have occurred during the evolution of the PIP5K locus and may aid in understanding the functional role of this gene in the cellular biology of apicomplexan parasites.

UR - http://www.scopus.com/inward/record.url?scp=79955936159&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79955936159&partnerID=8YFLogxK

U2 - 10.1007/s00436-010-2104-7

DO - 10.1007/s00436-010-2104-7

M3 - Article

VL - 108

SP - 611

EP - 620

JO - Zeitschrift fur Parasitenkunde

JF - Zeitschrift fur Parasitenkunde

SN - 0932-0113

IS - 3

ER -