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Protein tyrosine phosphatases encoded in Cotesia plutellae bracovirus: sequence analysis, expression profile, and a possible biological role in host immunosuppression.
Dev Comp Immunol. 2007; 31(10):978-90.DC

Abstract

A genome project has been launched and aims to sequence total genome of Cotesia plutellae bracovirus (CpBV). On this process, several putative open reading frames have been proposed, among which there was a large gene family coding for protein tyrosine phosphatases (PTPs). This study analyzed the deduced amino acid sequences of 14 CpBV-PTPs in terms of conserved domains with other known polydnaviral PTPs and determined their expression patterns in diamondback moth, Plutella xylostella, parasitized by C. plutellae. The analyzed CpBV-PTPs share the common 10 motifs with classical type of PTPs. However, there are variations among CpBV-PTPs in active site sequence and phosphorylation sites. Quantitative real-time polymerase chain reaction (PCR) indicated that most PTPs in the parasitized P. xylostella were expressed from the first day of parasitization and increased the expression levels during parasitization. All 14 PTPs were expressed in both immune-associated tissues of fat body and hemocytes in the parasitized host. During last instar, the PTP enzyme activity of the parasitized P. xylostella was significantly lower than that of the nonparasitized. The reduction of the PTP activity was observed in cytosolic fraction, but not in membrane fraction. The hemocytes of parasitized P. xylostella markedly lost their spreading ability in response to a cytokine (PSP1: plasmatocyte-spreading peptide 1). The functional link between the reduced PTP activity and the suppressed hemocytic behavior was evidenced by the inhibitory effect of sodium orthovanadate (a specific PTP inhibitor) on hemocyte-spreading behavior of nonparasitized P. xylostella. These results suggest that CpBV-PTPs are expressed in the parasitized P. xylostella and affect cellular PTP activity, which may be associated with host immunosuppression.

Authors+Show Affiliations

Department of Bioresource Sciences, Andong National University, Andong 760-749, Republic of Korea.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17363054

Citation

Ibrahim, Ahmed M A., et al. "Protein Tyrosine Phosphatases Encoded in Cotesia Plutellae Bracovirus: Sequence Analysis, Expression Profile, and a Possible Biological Role in Host Immunosuppression." Developmental and Comparative Immunology, vol. 31, no. 10, 2007, pp. 978-90.
Ibrahim AM, Choi JY, Je YH, et al. Protein tyrosine phosphatases encoded in Cotesia plutellae bracovirus: sequence analysis, expression profile, and a possible biological role in host immunosuppression. Dev Comp Immunol. 2007;31(10):978-90.
Ibrahim, A. M., Choi, J. Y., Je, Y. H., & Kim, Y. (2007). Protein tyrosine phosphatases encoded in Cotesia plutellae bracovirus: sequence analysis, expression profile, and a possible biological role in host immunosuppression. Developmental and Comparative Immunology, 31(10), 978-90.
Ibrahim AM, et al. Protein Tyrosine Phosphatases Encoded in Cotesia Plutellae Bracovirus: Sequence Analysis, Expression Profile, and a Possible Biological Role in Host Immunosuppression. Dev Comp Immunol. 2007;31(10):978-90. PubMed PMID: 17363054.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Protein tyrosine phosphatases encoded in Cotesia plutellae bracovirus: sequence analysis, expression profile, and a possible biological role in host immunosuppression. AU - Ibrahim,Ahmed M A, AU - Choi,Jae Young, AU - Je,Yeon Ho, AU - Kim,Yonggyun, Y1 - 2006/12/13/ PY - 2006/09/23/received PY - 2006/11/06/revised PY - 2006/11/09/accepted PY - 2007/3/17/pubmed PY - 2007/10/11/medline PY - 2007/3/17/entrez SP - 978 EP - 90 JF - Developmental and comparative immunology JO - Dev Comp Immunol VL - 31 IS - 10 N2 - A genome project has been launched and aims to sequence total genome of Cotesia plutellae bracovirus (CpBV). On this process, several putative open reading frames have been proposed, among which there was a large gene family coding for protein tyrosine phosphatases (PTPs). This study analyzed the deduced amino acid sequences of 14 CpBV-PTPs in terms of conserved domains with other known polydnaviral PTPs and determined their expression patterns in diamondback moth, Plutella xylostella, parasitized by C. plutellae. The analyzed CpBV-PTPs share the common 10 motifs with classical type of PTPs. However, there are variations among CpBV-PTPs in active site sequence and phosphorylation sites. Quantitative real-time polymerase chain reaction (PCR) indicated that most PTPs in the parasitized P. xylostella were expressed from the first day of parasitization and increased the expression levels during parasitization. All 14 PTPs were expressed in both immune-associated tissues of fat body and hemocytes in the parasitized host. During last instar, the PTP enzyme activity of the parasitized P. xylostella was significantly lower than that of the nonparasitized. The reduction of the PTP activity was observed in cytosolic fraction, but not in membrane fraction. The hemocytes of parasitized P. xylostella markedly lost their spreading ability in response to a cytokine (PSP1: plasmatocyte-spreading peptide 1). The functional link between the reduced PTP activity and the suppressed hemocytic behavior was evidenced by the inhibitory effect of sodium orthovanadate (a specific PTP inhibitor) on hemocyte-spreading behavior of nonparasitized P. xylostella. These results suggest that CpBV-PTPs are expressed in the parasitized P. xylostella and affect cellular PTP activity, which may be associated with host immunosuppression. SN - 0145-305X UR - https://www.unboundmedicine.com/medline/citation/17363054/Protein_tyrosine_phosphatases_encoded_in_Cotesia_plutellae_bracovirus:_sequence_analysis_expression_profile_and_a_possible_biological_role_in_host_immunosuppression_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0145-305X(06)00211-4 DB - PRIME DP - Unbound Medicine ER -