Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase

Y. Zhou; X. W. Lin; M. A. Begum; C. H. Zhang; X. X. Shi; W. J. Jiao; Y. R. Zhang; J. Q. Yuan; H. Y. Li; Q. Yang; C. Mao; Z. R. Zhu

doi:10.1111/imb.12302

Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase

Y. Zhou
, X. W. Lin
, M. A. Begum
, C. H. Zhang
, X. X. Shi
, W. J. Jiao
, Y. R. Zhang
, J. Q. Yuan
, H. Y. Li
, Q. Yang
, C. Mao
, Z. R. Zhu

Medicine, Chair

Stony Brook University

Zhejiang University
CAS - South China Institute of Botany
Jiangsu Academy of Agricultural Sciences

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

The neutral sphingomyelinase (nSMase) 1 homologue gene LsSMase was cloned from Laodelphax striatellus, a direct sap-sucker and virus vector of gramineous plants, and expressed via a Bac to Bac baculovirus expression system. The LsSMase-enhanced green fluorescent protein fusion protein was located in the endoplasmic reticulum in a similar manner to mammalian nSMase 1. The biochemical properties of LsSMase were determined in detail. The optimal pH and temperature for recombinant LsSMase were 8 and 37 °C, respectively. LsSMase was an Mg²⁺ or Mn²⁺ dependent enzyme, but different concentration of each were needed. The activity of LsSMase was significantly stimulated by Ethylene glycol bis(2-aminoethyl ether)tetraacetic acid (EGTA), whereas it was inhibited by ethylenediaminetetraacetic acid. Millimolar concentrations of Zn²⁺ completely inhibited LsSMase. The reducing agents dithiothreitol and β-mercaptoethanol varied in their effects on activity. Phospholipids were not found to stimulate LsSMase.

Original language	English
Pages (from-to)	392-402
Number of pages	11
Journal	Insect Molecular Biology
Volume	26
Issue number	4
DOIs	https://doi.org/10.1111/imb.12302
State	Published - Aug 2017

Keywords

Laodelphax striatellus
insect
sphingolipid
sphingomyelinase

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10.1111/imb.12302

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title = "Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase",

abstract = "The neutral sphingomyelinase (nSMase) 1 homologue gene LsSMase was cloned from Laodelphax striatellus, a direct sap-sucker and virus vector of gramineous plants, and expressed via a Bac to Bac baculovirus expression system. The LsSMase-enhanced green fluorescent protein fusion protein was located in the endoplasmic reticulum in a similar manner to mammalian nSMase 1. The biochemical properties of LsSMase were determined in detail. The optimal pH and temperature for recombinant LsSMase were 8 and 37 °C, respectively. LsSMase was an Mg2+ or Mn2+ dependent enzyme, but different concentration of each were needed. The activity of LsSMase was significantly stimulated by Ethylene glycol bis(2-aminoethyl ether)tetraacetic acid (EGTA), whereas it was inhibited by ethylenediaminetetraacetic acid. Millimolar concentrations of Zn2+ completely inhibited LsSMase. The reducing agents dithiothreitol and β-mercaptoethanol varied in their effects on activity. Phospholipids were not found to stimulate LsSMase.",

keywords = "Laodelphax striatellus, insect, sphingolipid, sphingomyelinase",

author = "Y. Zhou and Lin, \{X. W.\} and Begum, \{M. A.\} and Zhang, \{C. H.\} and Shi, \{X. X.\} and Jiao, \{W. J.\} and Zhang, \{Y. R.\} and Yuan, \{J. Q.\} and Li, \{H. Y.\} and Q. Yang and C. Mao and Zhu, \{Z. R.\}",

note = "Publisher Copyright: {\textcopyright} 2017 The Royal Entomological Society",

year = "2017",

month = aug,

doi = "10.1111/imb.12302",

language = "English",

volume = "26",

pages = "392--402",

journal = "Insect Molecular Biology",

issn = "0962-1075",

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number = "4",

}

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T1 - Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase

AU - Zhou, Y.

AU - Lin, X. W.

AU - Begum, M. A.

AU - Zhang, C. H.

AU - Shi, X. X.

AU - Jiao, W. J.

AU - Zhang, Y. R.

AU - Yuan, J. Q.

AU - Li, H. Y.

AU - Yang, Q.

AU - Mao, C.

AU - Zhu, Z. R.

PY - 2017/8

Y1 - 2017/8

N2 - The neutral sphingomyelinase (nSMase) 1 homologue gene LsSMase was cloned from Laodelphax striatellus, a direct sap-sucker and virus vector of gramineous plants, and expressed via a Bac to Bac baculovirus expression system. The LsSMase-enhanced green fluorescent protein fusion protein was located in the endoplasmic reticulum in a similar manner to mammalian nSMase 1. The biochemical properties of LsSMase were determined in detail. The optimal pH and temperature for recombinant LsSMase were 8 and 37 °C, respectively. LsSMase was an Mg2+ or Mn2+ dependent enzyme, but different concentration of each were needed. The activity of LsSMase was significantly stimulated by Ethylene glycol bis(2-aminoethyl ether)tetraacetic acid (EGTA), whereas it was inhibited by ethylenediaminetetraacetic acid. Millimolar concentrations of Zn2+ completely inhibited LsSMase. The reducing agents dithiothreitol and β-mercaptoethanol varied in their effects on activity. Phospholipids were not found to stimulate LsSMase.

AB - The neutral sphingomyelinase (nSMase) 1 homologue gene LsSMase was cloned from Laodelphax striatellus, a direct sap-sucker and virus vector of gramineous plants, and expressed via a Bac to Bac baculovirus expression system. The LsSMase-enhanced green fluorescent protein fusion protein was located in the endoplasmic reticulum in a similar manner to mammalian nSMase 1. The biochemical properties of LsSMase were determined in detail. The optimal pH and temperature for recombinant LsSMase were 8 and 37 °C, respectively. LsSMase was an Mg2+ or Mn2+ dependent enzyme, but different concentration of each were needed. The activity of LsSMase was significantly stimulated by Ethylene glycol bis(2-aminoethyl ether)tetraacetic acid (EGTA), whereas it was inhibited by ethylenediaminetetraacetic acid. Millimolar concentrations of Zn2+ completely inhibited LsSMase. The reducing agents dithiothreitol and β-mercaptoethanol varied in their effects on activity. Phospholipids were not found to stimulate LsSMase.

KW - Laodelphax striatellus

KW - insect

KW - sphingolipid

KW - sphingomyelinase

UR - https://www.scopus.com/pages/publications/85017377392

U2 - 10.1111/imb.12302

DO - 10.1111/imb.12302

M3 - Article

C2 - 28374513

SN - 0962-1075

VL - 26

SP - 392

EP - 402

JO - Insect Molecular Biology

JF - Insect Molecular Biology

IS - 4

ER -

Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase

Abstract

Keywords

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