Molecular characterisation of a candidate gut sucrase in the pea aphid, Acyrthosiphon pisum

D. R. G. Price; A. J. Karley; D. A. Ashford; H. V. Isaacs; M. E. Pownall; H. S. Wilkinson; J. A. Gatehouse; A. E. Douglas

doi:10.1016/j.ibmb.2006.12.005

Molecular characterisation of a candidate gut sucrase in the pea aphid, Acyrthosiphon pisum

D. R. G. Price, A. J. Karley, D. A. Ashford, H. V. Isaacs, M. E. Pownall, H. S. Wilkinson, J. A. Gatehouse, A. E. Douglas

Biology

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

Abstract

The hydrolysis of sucrose, the principal dietary source of carbon for aphids, is catalysed by a gut alpha-glucosidase/transglucosidase activity. An alpha-glucosidase, referred to as APS1, was identified in both a gut-specific cDNA library and a sucrase-enriched membrane preparation from guts of the pea aphid Acyrthosiphon pisum by a combination of genomic and proteomic techniques. APS1 contains a predicted signal peptide, and has a predicted molecular mass of 68 kDa (unprocessed) or 66.4 kDa (mature protein). It has amino acid sequence similarity to alpha-glucosidases (EC 3.2.1.20) of glycoside hydrolase family 13 in other insects. The predicted APS1 protein contains two domains: an N-terminal catalytic domain, and a C-terminal hydrophobic domain. In situ localisation and RT-PCR studies revealed that APS1 mRNA was expressed in the gut distal to the stomach, the same localisation as sucrase activity. When expressed heterologously in Xenopus embryos, APS1 was membrane-bound and had sucrase activity. It is concluded that APS1 is a dominant, and possibly sole, protein mediating sucrase activity in the aphid gut. (c) 2007 Published by Elsevier Ltd.

Original language	English
Pages (from-to)	307-317
Number of pages	11
Journal	Insect Biochemistry and Molecular Biology
Volume	37
Issue number	4
DOIs	https://doi.org/10.1016/j.ibmb.2006.12.005
Publication status	Published - Apr 2007

Keywords

Acyrthosiphon pisum
aphid
alpha-glucosidase
digestive enzyme
phloem-feeding insect
sucrase
PHLOEM-FEEDING INSECT
PERIMICROVILLAR MEMBRANES
NEISSERIA-POLYSACCHAREA
HONEYDEW
OSMOREGULATION
MIDGUT
SUCROSE
OLIGOSACCHARIDES
AMYLOSUCRASE
PROTEINS

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10.1016/j.ibmb.2006.12.005

http://dx.doi.org/10.1016/j.ibmb.2006.12.005

Cite this

@article{9d813fa277df48a1bd40ce671abc1c95,

title = "Molecular characterisation of a candidate gut sucrase in the pea aphid, Acyrthosiphon pisum",

abstract = "The hydrolysis of sucrose, the principal dietary source of carbon for aphids, is catalysed by a gut alpha-glucosidase/transglucosidase activity. An alpha-glucosidase, referred to as APS1, was identified in both a gut-specific cDNA library and a sucrase-enriched membrane preparation from guts of the pea aphid Acyrthosiphon pisum by a combination of genomic and proteomic techniques. APS1 contains a predicted signal peptide, and has a predicted molecular mass of 68 kDa (unprocessed) or 66.4 kDa (mature protein). It has amino acid sequence similarity to alpha-glucosidases (EC 3.2.1.20) of glycoside hydrolase family 13 in other insects. The predicted APS1 protein contains two domains: an N-terminal catalytic domain, and a C-terminal hydrophobic domain. In situ localisation and RT-PCR studies revealed that APS1 mRNA was expressed in the gut distal to the stomach, the same localisation as sucrase activity. When expressed heterologously in Xenopus embryos, APS1 was membrane-bound and had sucrase activity. It is concluded that APS1 is a dominant, and possibly sole, protein mediating sucrase activity in the aphid gut. (c) 2007 Published by Elsevier Ltd.",

keywords = "Acyrthosiphon pisum, aphid, alpha-glucosidase, digestive enzyme, phloem-feeding insect, sucrase, PHLOEM-FEEDING INSECT, PERIMICROVILLAR MEMBRANES, NEISSERIA-POLYSACCHAREA, HONEYDEW, OSMOREGULATION, MIDGUT, SUCROSE, OLIGOSACCHARIDES, AMYLOSUCRASE, PROTEINS",

author = "Price, {D. R. G.} and Karley, {A. J.} and Ashford, {D. A.} and Isaacs, {H. V.} and Pownall, {M. E.} and Wilkinson, {H. S.} and Gatehouse, {J. A.} and Douglas, {A. E.}",

year = "2007",

month = apr,

doi = "10.1016/j.ibmb.2006.12.005",

language = "English",

volume = "37",

pages = "307--317",

journal = "Insect Biochemistry and Molecular Biology",

issn = "0965-1748",

publisher = "Elsevier",

number = "4",

}

TY - JOUR

T1 - Molecular characterisation of a candidate gut sucrase in the pea aphid, Acyrthosiphon pisum

AU - Price, D. R. G.

AU - Karley, A. J.

AU - Ashford, D. A.

AU - Isaacs, H. V.

AU - Pownall, M. E.

AU - Wilkinson, H. S.

AU - Gatehouse, J. A.

AU - Douglas, A. E.

PY - 2007/4

Y1 - 2007/4

N2 - The hydrolysis of sucrose, the principal dietary source of carbon for aphids, is catalysed by a gut alpha-glucosidase/transglucosidase activity. An alpha-glucosidase, referred to as APS1, was identified in both a gut-specific cDNA library and a sucrase-enriched membrane preparation from guts of the pea aphid Acyrthosiphon pisum by a combination of genomic and proteomic techniques. APS1 contains a predicted signal peptide, and has a predicted molecular mass of 68 kDa (unprocessed) or 66.4 kDa (mature protein). It has amino acid sequence similarity to alpha-glucosidases (EC 3.2.1.20) of glycoside hydrolase family 13 in other insects. The predicted APS1 protein contains two domains: an N-terminal catalytic domain, and a C-terminal hydrophobic domain. In situ localisation and RT-PCR studies revealed that APS1 mRNA was expressed in the gut distal to the stomach, the same localisation as sucrase activity. When expressed heterologously in Xenopus embryos, APS1 was membrane-bound and had sucrase activity. It is concluded that APS1 is a dominant, and possibly sole, protein mediating sucrase activity in the aphid gut. (c) 2007 Published by Elsevier Ltd.

AB - The hydrolysis of sucrose, the principal dietary source of carbon for aphids, is catalysed by a gut alpha-glucosidase/transglucosidase activity. An alpha-glucosidase, referred to as APS1, was identified in both a gut-specific cDNA library and a sucrase-enriched membrane preparation from guts of the pea aphid Acyrthosiphon pisum by a combination of genomic and proteomic techniques. APS1 contains a predicted signal peptide, and has a predicted molecular mass of 68 kDa (unprocessed) or 66.4 kDa (mature protein). It has amino acid sequence similarity to alpha-glucosidases (EC 3.2.1.20) of glycoside hydrolase family 13 in other insects. The predicted APS1 protein contains two domains: an N-terminal catalytic domain, and a C-terminal hydrophobic domain. In situ localisation and RT-PCR studies revealed that APS1 mRNA was expressed in the gut distal to the stomach, the same localisation as sucrase activity. When expressed heterologously in Xenopus embryos, APS1 was membrane-bound and had sucrase activity. It is concluded that APS1 is a dominant, and possibly sole, protein mediating sucrase activity in the aphid gut. (c) 2007 Published by Elsevier Ltd.

KW - Acyrthosiphon pisum

KW - aphid

KW - alpha-glucosidase

KW - digestive enzyme

KW - phloem-feeding insect

KW - sucrase

KW - PHLOEM-FEEDING INSECT

KW - PERIMICROVILLAR MEMBRANES

KW - NEISSERIA-POLYSACCHAREA

KW - HONEYDEW

KW - OSMOREGULATION

KW - MIDGUT

KW - SUCROSE

KW - OLIGOSACCHARIDES

KW - AMYLOSUCRASE

KW - PROTEINS

U2 - 10.1016/j.ibmb.2006.12.005

DO - 10.1016/j.ibmb.2006.12.005

M3 - Article

SN - 0965-1748

VL - 37

SP - 307

EP - 317

JO - Insect Biochemistry and Molecular Biology

JF - Insect Biochemistry and Molecular Biology

IS - 4

ER -