Abstract
The present study addresses the cloning and characterization of a Cryptosporidium parvum antigen, CP2. Sequencing of cDNA and genomic clones revealed a novel gene capable of coding a message of 2,136 nucleotides flanked by 28 and 140 nucleotides of the 5′-and 3′-noncoding regions, respectively. The deduced amino acid sequence suggests that CP2 is a secreted and/ or membrane protein. Immunofluorescence microscopy detected CP2 enrichment in sporozoites that subsequently appeared to encase type I meronts in infected HCT-8 cells. Immunogold electron microscopy revealed that CP2 consistently localized to membranous structures throughout development. In addition, progression from macrogametocyte to sporulated oocyst revealed CP2 initially at the periphery of amylopectin-like granules, in the cytoplasm and discrete vesicles, the parasitophorous vacuole, on the surface of sporozoites, and finally on the parasitophorous vacuole membrane (PVM). The observed expression pattern suggests that CP2 may be involved in the invasion process and/or PVM integrity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 317-327 |
| Number of pages | 11 |
| Journal | Parasitology Research |
| Volume | 92 |
| Issue number | 4 |
| DOIs | |
| State | Published - Mar 2004 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Parasitology
Cite this
A novel Cryptosporidium parvum antigen, CP2, preferentially associates with membranous structures. / O'Hara, Steven P.; Yu, Jae R.; Lin, J. J C.
In: Parasitology Research, Vol. 92, No. 4, 03.2004, p. 317-327.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A novel Cryptosporidium parvum antigen, CP2, preferentially associates with membranous structures
AU - O'Hara, Steven P.
AU - Yu, Jae R.
AU - Lin, J. J C
PY - 2004/3
Y1 - 2004/3
N2 - The present study addresses the cloning and characterization of a Cryptosporidium parvum antigen, CP2. Sequencing of cDNA and genomic clones revealed a novel gene capable of coding a message of 2,136 nucleotides flanked by 28 and 140 nucleotides of the 5′-and 3′-noncoding regions, respectively. The deduced amino acid sequence suggests that CP2 is a secreted and/ or membrane protein. Immunofluorescence microscopy detected CP2 enrichment in sporozoites that subsequently appeared to encase type I meronts in infected HCT-8 cells. Immunogold electron microscopy revealed that CP2 consistently localized to membranous structures throughout development. In addition, progression from macrogametocyte to sporulated oocyst revealed CP2 initially at the periphery of amylopectin-like granules, in the cytoplasm and discrete vesicles, the parasitophorous vacuole, on the surface of sporozoites, and finally on the parasitophorous vacuole membrane (PVM). The observed expression pattern suggests that CP2 may be involved in the invasion process and/or PVM integrity.
AB - The present study addresses the cloning and characterization of a Cryptosporidium parvum antigen, CP2. Sequencing of cDNA and genomic clones revealed a novel gene capable of coding a message of 2,136 nucleotides flanked by 28 and 140 nucleotides of the 5′-and 3′-noncoding regions, respectively. The deduced amino acid sequence suggests that CP2 is a secreted and/ or membrane protein. Immunofluorescence microscopy detected CP2 enrichment in sporozoites that subsequently appeared to encase type I meronts in infected HCT-8 cells. Immunogold electron microscopy revealed that CP2 consistently localized to membranous structures throughout development. In addition, progression from macrogametocyte to sporulated oocyst revealed CP2 initially at the periphery of amylopectin-like granules, in the cytoplasm and discrete vesicles, the parasitophorous vacuole, on the surface of sporozoites, and finally on the parasitophorous vacuole membrane (PVM). The observed expression pattern suggests that CP2 may be involved in the invasion process and/or PVM integrity.
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UR - http://www.scopus.com/inward/citedby.url?scp=1542614372&partnerID=8YFLogxK
U2 - 10.1007/s00436-003-1057-5
DO - 10.1007/s00436-003-1057-5
M3 - Article
VL - 92
SP - 317
EP - 327
JO - Parasitology Research
JF - Parasitology Research
SN - 0932-0113
IS - 4
ER -