Niemann-Pick C2 Proteins: A New Function for an Old Family

Niemann-Pick proteins type C2 (NPC2) are carriers of cholesterol in vertebrates, with a single member in each species. The high sequence conservation between mammals and across vertebrates is related to their common function. In contrast, NPC2 proteins in arthropods have undergone extensive duplicat...

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Main Authors: Jiao Zhu, Mengbuo Guo, Liping Ban, Li-Mei Song, Yang Liu, Paolo Pelosi, Guirong Wang
Format: Article
Language:English
Published: Frontiers Media S.A. 2018-01-01
Series:Frontiers in Physiology
Subjects:
Online Access:http://journal.frontiersin.org/article/10.3389/fphys.2018.00052/full
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spelling doaj-58dfc45a00704f6baf68fb3bb9647a732020-11-25T00:10:44ZengFrontiers Media S.A.Frontiers in Physiology1664-042X2018-01-01910.3389/fphys.2018.00052333006Niemann-Pick C2 Proteins: A New Function for an Old FamilyJiao Zhu0Mengbuo Guo1Liping Ban2Li-Mei Song3Yang Liu4Paolo Pelosi5Guirong Wang6State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, ChinaState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, ChinaDepartment of Grassland Science, College of Animal Science and Technology, China Agricultural University, Beijing, ChinaDepartment of Grassland Science, College of Animal Science and Technology, China Agricultural University, Beijing, ChinaState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, ChinaState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, ChinaState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, ChinaNiemann-Pick proteins type C2 (NPC2) are carriers of cholesterol in vertebrates, with a single member in each species. The high sequence conservation between mammals and across vertebrates is related to their common function. In contrast, NPC2 proteins in arthropods have undergone extensive duplication and differentiation, probably under environmental pressure, and are likely to have different functions. Recent studies have suggested that in arthropods these proteins might act as carriers for semiochemicals and other hydrophobic compounds. In this study we focused on the function of a specific NPC2 gene in the moth Helicoverpa armigera (HarmNPC2-1). This protein binds several flavonoids with micromolar dissociation constants. The best ligand was gossypol, present in cotton, one of the main host plants for H. armigera. Western blot revealed the presence of HarmNPC2-1 in different parts of the body, including the antennae, proboscis, and abdomen. In the antennae, in situ hybridization experiments produced strong staining in auxiliary cells at the base of sensilla trichodea, basiconica, coeloconica, and chaetica. Immunocytochemistry confirmed the expression of the protein in sensilla chaetica. Our results support a role of semiochemical carriers for NPC2 proteins in insects and indicate such proteins as new targets for insecticide-free pest population control.http://journal.frontiersin.org/article/10.3389/fphys.2018.00052/fullNiemann-Pick protein C2LepidopteraHelicoverpa armigerain situ hybridizationimmunocytochemistryligand-binding
collection DOAJ
language English
format Article
sources DOAJ
author Jiao Zhu
Mengbuo Guo
Liping Ban
Li-Mei Song
Yang Liu
Paolo Pelosi
Guirong Wang
spellingShingle Jiao Zhu
Mengbuo Guo
Liping Ban
Li-Mei Song
Yang Liu
Paolo Pelosi
Guirong Wang
Niemann-Pick C2 Proteins: A New Function for an Old Family
Frontiers in Physiology
Niemann-Pick protein C2
Lepidoptera
Helicoverpa armigera
in situ hybridization
immunocytochemistry
ligand-binding
author_facet Jiao Zhu
Mengbuo Guo
Liping Ban
Li-Mei Song
Yang Liu
Paolo Pelosi
Guirong Wang
author_sort Jiao Zhu
title Niemann-Pick C2 Proteins: A New Function for an Old Family
title_short Niemann-Pick C2 Proteins: A New Function for an Old Family
title_full Niemann-Pick C2 Proteins: A New Function for an Old Family
title_fullStr Niemann-Pick C2 Proteins: A New Function for an Old Family
title_full_unstemmed Niemann-Pick C2 Proteins: A New Function for an Old Family
title_sort niemann-pick c2 proteins: a new function for an old family
publisher Frontiers Media S.A.
series Frontiers in Physiology
issn 1664-042X
publishDate 2018-01-01
description Niemann-Pick proteins type C2 (NPC2) are carriers of cholesterol in vertebrates, with a single member in each species. The high sequence conservation between mammals and across vertebrates is related to their common function. In contrast, NPC2 proteins in arthropods have undergone extensive duplication and differentiation, probably under environmental pressure, and are likely to have different functions. Recent studies have suggested that in arthropods these proteins might act as carriers for semiochemicals and other hydrophobic compounds. In this study we focused on the function of a specific NPC2 gene in the moth Helicoverpa armigera (HarmNPC2-1). This protein binds several flavonoids with micromolar dissociation constants. The best ligand was gossypol, present in cotton, one of the main host plants for H. armigera. Western blot revealed the presence of HarmNPC2-1 in different parts of the body, including the antennae, proboscis, and abdomen. In the antennae, in situ hybridization experiments produced strong staining in auxiliary cells at the base of sensilla trichodea, basiconica, coeloconica, and chaetica. Immunocytochemistry confirmed the expression of the protein in sensilla chaetica. Our results support a role of semiochemical carriers for NPC2 proteins in insects and indicate such proteins as new targets for insecticide-free pest population control.
topic Niemann-Pick protein C2
Lepidoptera
Helicoverpa armigera
in situ hybridization
immunocytochemistry
ligand-binding
url http://journal.frontiersin.org/article/10.3389/fphys.2018.00052/full
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