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pmid:26543889

Combining two-dimensional gel electrophoresis and metabolomic data in support of dry-season survival in the two main species of the malarial mosquito Anopheles gambiae.

K Hidalgo · K Mouline · W Mamai · N Foucreau · K R Dabiré · A Bouchereau · F Simard · D Renault

Data in brief · 2015 doi:10.1016/j.dib.2015.08.031

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Record details sci_version · id · kind · revision · content_hash · schema · created_at · updated_at · generator
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pmid:26543889
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2026-11-01T15:40:13Z
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title
Combining two-dimensional gel electrophoresis and metabolomic data in support of dry-season survival in the two main species of the malarial mosquito Anopheles gambiae.
doi
10.1016/j.dib.2015.08.031
pmid
26543889
authors array · 8 items
[0]
K Hidalgo
[1]
K Mouline
[2]
W Mamai
[3]
N Foucreau
[4]
K R Dabiré
[5]
A Bouchereau
[6]
F Simard
[7]
D Renault
journal
Data in brief
year
2015
abstract
In dry savannahs of West-Africa, the malarial mosquitoes of the Anopheles gambiae sensu stricto complex annually survive the harsh desiccating conditions of the dry season. However, the physiological and biochemical mechanisms underlying how these mosquitoes survive such desiccating conditions are still undefined, and controversial. In this context, we provide the first work examining both proteomic and metabolomic changes in the two molecular forms of A. gambiae s.s (M and S forms) experimentally exposed to the rainy and dry season conditions as they experience in the field. Protein abundances of the mosquitoes were measured using a two-dimensional fluorescence difference gel electrophoresis (2D DIGE) coupled with a matrix-assisted laser desorption/ionisation-time of flight (MALDI-TOF) and tandem mass spectrometry (MS) for protein identification. These assays were conducted by Applied Biomics (http://www.appliedbiomics.com, Applied Biomics, Inc. Hayward, CA, USA), and the mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000294. The metabolomic analysis was conducted using both Acquity UPLC(®) system (for amino acid identification), and a gas-chromatography-mass spectrometry platform (for sugars identification). Metabolomic fingerprintings were assessed in the University of Rennes 1, UMR CNRS 6553 EcoBio (France). A detailed interpretation of the obtained data can be found in Hidalgo et al. (2014) [1] (Journal of Insect Physiology (2014)).
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Then, images were subjected to in-gel analysis and cross-gel analysis using DeCyder v6.5 (GE-Healthcare) with a P-value <0.05 according to Student’s t-tests.
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sections[12] "3.4. Image analysis" paragraph 2
quote
Then, images were subjected to in-gel analysis and cross-gel analysis using DeCyder v6.5 (GE-Healthcare) with a P-value <0.05 according to Student’s t-tests.
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The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000294.
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sections[2] "table-wrap" paragraph 1
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The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000294.
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The study provided the first examination of proteomic and metabolomic changes in M and S forms of Anopheles gambiae s.s exposed to rainy- and dry-season field conditions. Statistical analyses included Student’s t-tests, multivariate discriminant analyses, MANOVAs, Benjamini–Hochberg adjustment, Kruskal–Wallis tests, and Bonferroni correction. The mass spectrometry proteomics source data are accessible through ProteomeXchange via the PRIDE partner repository under dataset identifier PXD000294.
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sections[0] "Abstract" paragraph 1
quote
In this context, we provide the first work examining both proteomic and metabolomic changes in the two molecular forms of A. gambiae s.s (M and S forms) experimentally exposed to the rainy and dry season conditions as they experience in the field.
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sections[12] "3.4. Image analysis" paragraph 2
quote
Then, images were subjected to in-gel analysis and cross-gel analysis using DeCyder v6.5 (GE-Healthcare) with a P-value <0.05 according to Student’s t-tests.
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sections[20] "4.4.1. Amino acids" paragraph 2
quote
Significance of amino acid fingerprintings among species and rearing conditions was assessed using multivariate discriminant analyses and MANOVAs.
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sections[20] "4.4.1. Amino acids" paragraph 2
quote
Because false discovery rate can be induced by multiple comparisons, we used a Benjamini–Hochberg procedure to adjust all P-values.
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sections[21] "4.4.2. Sugars" paragraph 2
quote
Significance of the galactose and glucose concentrations variation among species and rearing conditions was assessed using Kruskal–Wallis tests, followed by a Bonferroni procedure resulting in a decreased threshold of significance from P-value <0.05 to P-value <0.01.
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sections[2] "table-wrap" paragraph 1
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The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000294.
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The study provided the first examination of proteomic and metabolomic changes in M and S forms of Anopheles gambiae s.s exposed to rainy- and dry-season field conditions. Statistical analyses included Student’s t-tests, multivariate discriminant analyses, MANOVAs, Benjamini–Hochberg adjustment, Kruskal–Wallis tests, and Bonferroni correction. The mass spectrometry proteomics source data are accessible through ProteomeXchange via the PRIDE partner repository under dataset identifier PXD000294.
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Novel insights into the metabolic and biochemical underpinnings assisting dry-season survival in female malaria mosquitoes of the Anopheles gambiae complex
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List of the 39 protein spots displaying differential abundance (average fold difference>1.3, absolute value; P<0.05) between the two rearing conditions in 1- h old female A. gambiae M and S, or between the two species whatever the rearing conditions. Adapted from Hidalgoet al. [1].
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3.5. Protein identification using matrix-assisted laser desorption/ionisation-time of flight (MALDI-TOF) and tandem mass spectrometry (MS)
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Table 1
caption
List of the 39 protein spots displaying differential abundance (average fold difference>1.3, absolute value; P<0.05) between the two rearing conditions in 1- h old female A. gambiae M and S, or between the two species whatever the rearing conditions. Adapted from Hidalgoet al. [1].
rows array · 40 items
[0] array · 7 items
[0]
Spot no.a
[1]
Protein name
[2]
Protein scoresb
[3]
No. Of matched peptides
[4]
Source species
[5]
Accession no.c
[6]
Functionsd
[1] array · 7 items
[0]
01
[1]
tropomyosin invertebrate
[2]
318
[3]
12
[4]
Culex quinquefasciatus
[5]
gi|170056897
[6]
Muscle contraction
[2] array · 7 items
[0]
02
[1]
hexamerin 2 beta
[2]
41
[3]
2
[4]
Aedes aegypti
[5]
gi|157119837
[6]
Storage of amino acid
[3] array · 7 items
[0]
03
[1]
arylphorin subunit alpha
[2]
134
[3]
4
[4]
Culex quinquefasciatus
[5]
gi|170043201
[6]
Storage of amino acid / Constituent of Cuticle sclerotizing system
[4] array · 7 items
[0]
07
[1]
hexamerin A
[2]
284
[3]
15
[4]
Anopheles melas
[5]
gi|3420171
[6]
Storage of amino acid
[5] array · 7 items
[0]
09
[1]
hypothetical protein AND_22551
[2]
153
[3]
15
[4]
Anopheles darlingi
[5]
gi|312371166
[6]
Storage of amino acid
[6] array · 7 items
[0]
12
[1]
hexamerin 2 beta
[2]
70
[3]
4
[4]
Aedes aegypti
[5]
gi|157110143
[6]
Storage of amino acid
[7] array · 7 items
[0]
13
[1]
myosin-Id
[2]
172
[3]
5
[4]
Culex quinquefasciatus
[5]
gi|170029188
[6]
Muscle contraction
[8] array · 7 items
[0]
19
[1]
catalase
[2]
215
[3]
16
[4]
Anopheles gambiae
[5]
gi|118638436
[6]
Response to oxidative stresses
[9] array · 7 items
[0]
21
[1]
hypothetical protein AND_22551
[2]
321
[3]
12
[4]
Anopheles darlingi
[5]
gi|312371166
[6]
Storage of amino acid
[10] array · 7 items
[0]
24
[1]
AGAP005558-PA
[2]
1000
[3]
19
[4]
Anopheles gambiae
[5]
gi|31213235
[6]
Proteolysis
[11] array · 7 items
[0]
25
[1]
AGAP005558-PA
[2]
570
[3]
16
[4]
Anopheles gambiae
[5]
gi|31213235
[6]
Proteolysis
[12] array · 7 items
[0]
27
[1]
aspartate ammonia lyase
[2]
301
[3]
15
[4]
Aedes aegypti
[5]
gi|157118058
[6]
Tricarboxylic acid cycle
[13] array · 7 items
[0]
37
[1]
myosin regulatory light chain 2 (mlc-2)
[2]
336
[3]
5
[4]
Aedes aegypti
[5]
gi|157167683
[6]
Muscle contraction
[14] array · 7 items
[0]
38
[1]
myosin regulatory light chain 2 (mlc-2)
[2]
299
[3]
5
[4]
Aedes aegypti
[5]
gi|157167683
[6]
Muscle contraction
[15] array · 7 items
[0]
39
[1]
myosin regulatory light chain 2 (mlc-2)
[2]
330
[3]
5
[4]
Aedes aegypti
[5]
gi|157167683
[6]
Muscle contraction
[16] array · 7 items
[0]
45
[1]
AGAP007963-PA
[2]
601
[3]
16
[4]
Anopheles gambiae
[5]
gi|118789564
[6]
Muscle contraction
[17] array · 7 items
[0]
52
[1]
ATP synthase beta subunit
[2]
250
[3]
12
[4]
Culex quinquefasciatus
[5]
gi|170040305
[6]
ATP synthesis
[18] array · 7 items
[0]
55
[1]
AGAP011284-PA
[2]
304
[3]
11
[4]
Anopheles gambiae
[5]
gi|118779554
[6]
Positive regulation of translational elongation and termination
[19] array · 7 items
[0]
56
[1]
NADH dehydrogenase
[2]
268
[3]
6
[4]
Culex quinquefasciatus
[5]
gi|170037145
[6]
Respiratory chain process
[20] array · 7 items
[0]
57
[1]
myosin light chain 1, putative
[2]
202
[3]
4
[4]
Aedes aegypti
[5]
gi|157167807
[6]
Muscle contraction
[21] array · 7 items
[0]
58
[1]
myosin light chain 1, putative
[2]
117
[3]
4
[4]
Aedes aegypti
[5]
gi|157167807
[6]
Muscle contraction
[22] array · 7 items
[0]
59
[1]
myosin light chain 1, putative
[2]
156
[3]
5
[4]
Aedes aegypti
[5]
gi|157167807
[6]
Muscle contraction
[23] array · 7 items
[0]
60
[1]
myosin light chain 1, putative
[2]
181
[3]
5
[4]
Aedes aegypti
[5]
gi|157167807
[6]
Muscle contraction
[24] array · 7 items
[0]
64
[1]
AGAP010657-PA
[2]
165
[3]
8
[4]
Anopheles gambiae str. PEST
[5]
gi|158289706
[6]
Oxygen transporter activity
[25] array · 7 items
[0]
65
[1]
⁎cuticular protein 117, RR-2 family (AGAP003379-PA)
[2]
709
[3]
9
[4]
Anopheles gambiae
[5]
gi|158290052
[6]
Structural constituent of the rigid cuticle
[26] array · 7 items
[0]
67
[1]
⁎cuticular protein 70, RR-2 family (AGAP006283-PB)
[2]
608
[3]
9
[4]
Anopheles gambiae
[5]
gi|158295676
[6]
Structural constituent of the rigid cuticle
[27] array · 7 items
[0]
68
[1]
hexamerin A
[2]
395
[3]
26
[4]
Anopheles gambiae
[5]
gi|3420159
[6]
Storage of amino acid
[28] array · 7 items
[0]
33
[1]
myosin heavy chain, nonmuscle or smooth muscle
[2]
124
[3]
17
[4]
Aedes aegypti
[5]
gi|157111095
[6]
Muscle contraction
[29] array · 7 items
[0]
73
[1]
myosin heavy chain, nonmuscle or smooth muscle
[2]
498
[3]
36
[4]
Aedes aegypti
[5]
gi|157110721
[6]
Muscle contraction
[30] array · 7 items
[0]
75
[1]
glycogen phosphorylase
[2]
635
[3]
21
[4]
Aedes aegypti
[5]
gi|157108521
[6]
Glycogenolysis process
[31] array · 7 items
[0]
76
[1]
prophenoloxidase
[2]
955
[3]
38
[4]
Anopheles gambiae
[5]
gi|3892092
[6]
Oxidation-reduction process
[32] array · 7 items
[0]
80
[1]
AGAP007393-PB
[2]
570
[3]
19
[4]
Anopheles gambiae str. PEST
[5]
gi|118778070
[6]
Cell redox homoeostasis / Glycerol ether metabolic process
[33] array · 7 items
[0]
84
[1]
citrate synthase
[2]
58
[3]
12
[4]
Aedes aegypti
[5]
gi|157133341
[6]
Tricarboxylic acid cycle
[34] array · 7 items
[0]
85
[1]
isocitrate dehydrogenase cytoplasmic
[2]
283
[3]
14
[4]
Culex quinquefasciatus
[5]
gi|170028051
[6]
Tricarboxylic acid cycle
[35] array · 7 items
[0]
92
[1]
AGAP009218-PA
[2]
141
[3]
4
[4]
Anopheles gambiae str. PEST
[5]
gi|118791868
[6]
Proteolysis
[36] array · 7 items
[0]
93
[1]
AGAP005423-PA
[2]
588
[3]
11
[4]
Anopheles gambiae str. PEST
[5]
gi|118786445
[6]
Ubiquitin-dependent protein catabolic process
[37] array · 7 items
[0]
96
[1]
arginine kinase
[2]
503
[3]
14
[4]
Mimomyia luzonensis
[5]
gi|284159531
[6]
Transferase / Kinase
[38] array · 7 items
[0]
99
[1]
glutathione transferase epsilon3
[2]
358
[3]
4
[4]
Anopheles dirus
[5]
gi|74275399
[6]
Transferase
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[0]
101
[1]
cuticular protein 123, RR-2 family (AGAP003385-PA)
[2]
814
[3]
9
[4]
Anopheles gambiae str. PEST
[5]
gi|158290062
[6]
Structural constituent of the rigid cuticle
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List of the 22 standard amino acids used for metabolomic assays.
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4.2. Identification and quantification of amino acids
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Table 2
caption
List of the 22 standard amino acids used for metabolomic assays.
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[0] array · 2 items
[0]
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[1]
abbreviation
[1] array · 2 items
[0]
Alanine
[1]
Ala
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[0]
Arginine
[1]
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[3] array · 2 items
[0]
Asparagine
[1]
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[4] array · 2 items
[0]
Aspartate
[1]
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[5] array · 2 items
[0]
Cystein
[1]
Cys
[6] array · 2 items
[0]
GABA
[1]
GABA
[7] array · 2 items
[0]
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[1]
Glu
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[0]
Glutamine
[1]
Gln
[9] array · 2 items
[0]
Glycine
[1]
Gly
[10] array · 2 items
[0]
Histidine
[1]
His
[11] array · 2 items
[0]
Isoleucine
[1]
Ile
[12] array · 2 items
[0]
Leucine
[1]
Leu
[13] array · 2 items
[0]
Lysine
[1]
Lys
[14] array · 2 items
[0]
Methionine
[1]
Met
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[0]
Ornithine
[1]
Orn
[16] array · 2 items
[0]
Phenylalanine
[1]
Phe
[17] array · 2 items
[0]
Proline
[1]
Pro
[18] array · 2 items
[0]
Serine
[1]
Ser
[19] array · 2 items
[0]
Threonine
[1]
Thr
[20] array · 2 items
[0]
Tryptophan
[1]
Trp
[21] array · 2 items
[0]
Tyrosine
[1]
Tyr
[22] array · 2 items
[0]
Valine
[1]
Val
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However, the physiological and biochemical mechanisms underlying how these mosquitoes survive such desiccating conditions are still undefined, and controversial. In this context, we provide the first work examining both proteomic and metabolomic changes in the two molecular forms of A. gambiae s.s (M and S forms) experimentally exposed to the rainy and dry season conditions as they experience in the field. Protein abundances of the mosquitoes were measured using a two-dimensional fluorescence difference gel electrophoresis (2D DIGE) coupled with a matrix-assisted laser desorption/ionisation-time of flight (MALDI-TOF) and tandem mass spectrometry (MS) for protein identification. These assays were conducted by Applied Biomics (http://www.appliedbiomics.com, Applied Biomics, Inc. Hayward, CA, USA), and the mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000294. The metabolomic analysis was conducted using both Acquity UPLC(®) system (for amino acid identification), and a gas-chromatography-mass spectrometry platform (for sugars identification). Metabolomic fingerprintings were assessed in the University of Rennes 1, UMR CNRS 6553 EcoBio (France). A detailed interpretation of the obtained data can be found in Hidalgo et al. (2014) [1] (Journal of Insect Physiology (2014)).", "claims": [{"id": "claim-method", "statement": "Then, images were subjected to in-gel analysis and cross-gel analysis using DeCyder v6.5 (GE-Healthcare) with a P-value <0.05 according to Student’s t-tests.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:26543889", "locator": "sections[12] \"3.4. 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