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Phenoloxidase in larvae of Plodia interpunctella (Lepidoptera: Pyralidae): molecular cloning of the proenzyme cDNA and enzyme activity in larvae paralyzed and parasitized by Habrobracon hebetor (Hymenoptera: Braconidae).
Arch Insect Biochem Physiol. 2005 Jun; 59(2):67-79.AI

Abstract

Phenoloxidase (PO) is a major component of the insect immune system. The enzyme is involved in encapsulation and melanization processes as well as wound healing and cuticle sclerotization. PO is present as an inactive proenzyme, prophenoloxidase (PPO), which is activated via a protease cascade. In this study, we have cloned a full-length PPO1 cDNA and a partial PPO2 cDNA from the Indianmeal moth, Plodia interpunctella (Hubner) (Lepidoptera: Pyralidae) and documented changes in PO activity in larvae paralyzed and parasitized by the ectoparasitoid Habrobracon hebetor (Say) (Hymenoptera: Braconidae). The cDNA for PPO1 is 2,748 bp and encodes a protein of 681 amino acids with a calculated molecular weight of 78,328 and pI of 6.41 containing a conserved proteolytic cleavage site found in other PPOs. P. interpunctella PPO1 ranges from 71-78% identical to other known lepidopteran PPO-1 sequences. Percent identity decreases as comparisons are made to PPO-1 of more divergent species in the orders Diptera (Aa-48; As-49; and Sb-60%) and Coleoptera (Tm-58; Hd-50%). Paralyzation of host larvae of P. interpunctella by the idiobiont H. hebetor results in an increase in phenoloxidase activity in host hemolymph, a process that may protect the host from microbial infection during self-provisioning by this wasp. Subsequent parasitization by H. hebetor larvae causes a decrease in hemolymph PO activity, which suggests that the larval parasitoid may be secreting an immunosuppressant into the host larva during feeding.

Authors+Show Affiliations

Department of Entomology, Kansas State University, Manhattan, Kansas 66506, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

15898113

Citation

Hartzer, Kris L., et al. "Phenoloxidase in Larvae of Plodia Interpunctella (Lepidoptera: Pyralidae): Molecular Cloning of the Proenzyme cDNA and Enzyme Activity in Larvae Paralyzed and Parasitized By Habrobracon Hebetor (Hymenoptera: Braconidae)." Archives of Insect Biochemistry and Physiology, vol. 59, no. 2, 2005, pp. 67-79.
Hartzer KL, Zhu KY, Baker JE. Phenoloxidase in larvae of Plodia interpunctella (Lepidoptera: Pyralidae): molecular cloning of the proenzyme cDNA and enzyme activity in larvae paralyzed and parasitized by Habrobracon hebetor (Hymenoptera: Braconidae). Arch Insect Biochem Physiol. 2005;59(2):67-79.
Hartzer, K. L., Zhu, K. Y., & Baker, J. E. (2005). Phenoloxidase in larvae of Plodia interpunctella (Lepidoptera: Pyralidae): molecular cloning of the proenzyme cDNA and enzyme activity in larvae paralyzed and parasitized by Habrobracon hebetor (Hymenoptera: Braconidae). Archives of Insect Biochemistry and Physiology, 59(2), 67-79.
Hartzer KL, Zhu KY, Baker JE. Phenoloxidase in Larvae of Plodia Interpunctella (Lepidoptera: Pyralidae): Molecular Cloning of the Proenzyme cDNA and Enzyme Activity in Larvae Paralyzed and Parasitized By Habrobracon Hebetor (Hymenoptera: Braconidae). Arch Insect Biochem Physiol. 2005;59(2):67-79. PubMed PMID: 15898113.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Phenoloxidase in larvae of Plodia interpunctella (Lepidoptera: Pyralidae): molecular cloning of the proenzyme cDNA and enzyme activity in larvae paralyzed and parasitized by Habrobracon hebetor (Hymenoptera: Braconidae). AU - Hartzer,Kris L, AU - Zhu,Kun Yan, AU - Baker,James E, PY - 2005/5/18/pubmed PY - 2005/8/2/medline PY - 2005/5/18/entrez SP - 67 EP - 79 JF - Archives of insect biochemistry and physiology JO - Arch Insect Biochem Physiol VL - 59 IS - 2 N2 - Phenoloxidase (PO) is a major component of the insect immune system. The enzyme is involved in encapsulation and melanization processes as well as wound healing and cuticle sclerotization. PO is present as an inactive proenzyme, prophenoloxidase (PPO), which is activated via a protease cascade. In this study, we have cloned a full-length PPO1 cDNA and a partial PPO2 cDNA from the Indianmeal moth, Plodia interpunctella (Hubner) (Lepidoptera: Pyralidae) and documented changes in PO activity in larvae paralyzed and parasitized by the ectoparasitoid Habrobracon hebetor (Say) (Hymenoptera: Braconidae). The cDNA for PPO1 is 2,748 bp and encodes a protein of 681 amino acids with a calculated molecular weight of 78,328 and pI of 6.41 containing a conserved proteolytic cleavage site found in other PPOs. P. interpunctella PPO1 ranges from 71-78% identical to other known lepidopteran PPO-1 sequences. Percent identity decreases as comparisons are made to PPO-1 of more divergent species in the orders Diptera (Aa-48; As-49; and Sb-60%) and Coleoptera (Tm-58; Hd-50%). Paralyzation of host larvae of P. interpunctella by the idiobiont H. hebetor results in an increase in phenoloxidase activity in host hemolymph, a process that may protect the host from microbial infection during self-provisioning by this wasp. Subsequent parasitization by H. hebetor larvae causes a decrease in hemolymph PO activity, which suggests that the larval parasitoid may be secreting an immunosuppressant into the host larva during feeding. SN - 0739-4462 UR - https://www.unboundmedicine.com/medline/citation/15898113/Phenoloxidase_in_larvae_of_Plodia_interpunctella__Lepidoptera:_Pyralidae_:_molecular_cloning_of_the_proenzyme_cDNA_and_enzyme_activity_in_larvae_paralyzed_and_parasitized_by_Habrobracon_hebetor__Hymenoptera:_Braconidae__ DB - PRIME DP - Unbound Medicine ER -