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Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera Culicidae)

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Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera Culicidae). / Sor-Suwan, Sriwatapron; Jariyapan, Narissara; Roytrakul, Sittiruk et al.
In: Parasitology Research, Vol. 112, No. 3, 2013, p. 1065-1075.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Sor-Suwan, S, Jariyapan, N, Roytrakul, S, Paemanee, A, Saeung, A, Thongsahuan, S, Phattanawiboon, B, Bates, PA, Poovorawan, Y & Choochote, W 2013, 'Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera Culicidae)', Parasitology Research, vol. 112, no. 3, pp. 1065-1075. https://doi.org/10.1007/s00436-012-3233-y

APA

Sor-Suwan, S., Jariyapan, N., Roytrakul, S., Paemanee, A., Saeung, A., Thongsahuan, S., Phattanawiboon, B., Bates, P. A., Poovorawan, Y., & Choochote, W. (2013). Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera Culicidae). Parasitology Research, 112(3), 1065-1075. https://doi.org/10.1007/s00436-012-3233-y

Vancouver

Sor-Suwan S, Jariyapan N, Roytrakul S, Paemanee A, Saeung A, Thongsahuan S et al. Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera Culicidae). Parasitology Research. 2013;112(3):1065-1075. doi: 10.1007/s00436-012-3233-y

Author

Sor-Suwan, Sriwatapron ; Jariyapan, Narissara ; Roytrakul, Sittiruk et al. / Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera Culicidae). In: Parasitology Research. 2013 ; Vol. 112, No. 3. pp. 1065-1075.

Bibtex

@article{d883114bd3024f27bc111275a33d7bc7,
title = "Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera Culicidae)",
abstract = "Anopheles campestris-like is proven to be a high-potential vector of Plasmodium vivax in Thailand. In this study, A. campestris-like salivary gland proteins were determined and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), two-dimensional gel electrophoresis, and nano-liquid chromatography-mass spectrometry. The total amount of salivary gland proteins in the mosquitoes aged 3-5 days was approximately 0.1 ± 0.05 μg/male and 1.38 ± 0.01 μg/female. SDS-PAGE analysis revealed at least 12 major proteins found in the female salivary glands and each morphological region of the female glands contained different major proteins. Two-dimensional gel electrophoresis showed approximately 20 major and several minor protein spots displaying relative molecular masses from 10 to 72 kDa with electric points ranging from 3.9 to 10. At least 15 glycoproteins were detected in the female glands. Similar electrophoretic protein profiles were detected comparing the male and proximal-lateral lobes of the female glands, suggesting that these lobes are responsible for sugar feeding. Blood-feeding proteins, i.e., putative 5'-nucleotidase/apyrase, anti-platelet protein, long-form D7 salivary protein, D7-related 1 protein, and gSG6, were detected in the distal-lateral lobes (DL) and/or medial lobes (ML) of the female glands. The major spots related to housekeeping proteins from other arthropod species including Culex quinquefasciatus serine/threonine-protein kinase rio3 expressed in both male and female glands, Ixodes scapularis putative sil1 expressed in DL and ML, and I. scapularis putative cyclophilin A expressed in DL. These results provide information for further study on the salivary gland proteins of A. campestris-like that are involved in hematophagy and disease transmission.",
author = "Sriwatapron Sor-Suwan and Narissara Jariyapan and Sittiruk Roytrakul and Atchara Paemanee and Atiporn Saeung and Sorawat Thongsahuan and Benjarat Phattanawiboon and Bates, {Paul A} and Yong Poovorawan and Wej Choochote",
year = "2013",
doi = "10.1007/s00436-012-3233-y",
language = "English",
volume = "112",
pages = "1065--1075",
journal = "Parasitology Research",
issn = "0044-3255",
publisher = "Springer Verlag",
number = "3",

}

RIS

TY - JOUR

T1 - Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera Culicidae)

AU - Sor-Suwan, Sriwatapron

AU - Jariyapan, Narissara

AU - Roytrakul, Sittiruk

AU - Paemanee, Atchara

AU - Saeung, Atiporn

AU - Thongsahuan, Sorawat

AU - Phattanawiboon, Benjarat

AU - Bates, Paul A

AU - Poovorawan, Yong

AU - Choochote, Wej

PY - 2013

Y1 - 2013

N2 - Anopheles campestris-like is proven to be a high-potential vector of Plasmodium vivax in Thailand. In this study, A. campestris-like salivary gland proteins were determined and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), two-dimensional gel electrophoresis, and nano-liquid chromatography-mass spectrometry. The total amount of salivary gland proteins in the mosquitoes aged 3-5 days was approximately 0.1 ± 0.05 μg/male and 1.38 ± 0.01 μg/female. SDS-PAGE analysis revealed at least 12 major proteins found in the female salivary glands and each morphological region of the female glands contained different major proteins. Two-dimensional gel electrophoresis showed approximately 20 major and several minor protein spots displaying relative molecular masses from 10 to 72 kDa with electric points ranging from 3.9 to 10. At least 15 glycoproteins were detected in the female glands. Similar electrophoretic protein profiles were detected comparing the male and proximal-lateral lobes of the female glands, suggesting that these lobes are responsible for sugar feeding. Blood-feeding proteins, i.e., putative 5'-nucleotidase/apyrase, anti-platelet protein, long-form D7 salivary protein, D7-related 1 protein, and gSG6, were detected in the distal-lateral lobes (DL) and/or medial lobes (ML) of the female glands. The major spots related to housekeeping proteins from other arthropod species including Culex quinquefasciatus serine/threonine-protein kinase rio3 expressed in both male and female glands, Ixodes scapularis putative sil1 expressed in DL and ML, and I. scapularis putative cyclophilin A expressed in DL. These results provide information for further study on the salivary gland proteins of A. campestris-like that are involved in hematophagy and disease transmission.

AB - Anopheles campestris-like is proven to be a high-potential vector of Plasmodium vivax in Thailand. In this study, A. campestris-like salivary gland proteins were determined and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), two-dimensional gel electrophoresis, and nano-liquid chromatography-mass spectrometry. The total amount of salivary gland proteins in the mosquitoes aged 3-5 days was approximately 0.1 ± 0.05 μg/male and 1.38 ± 0.01 μg/female. SDS-PAGE analysis revealed at least 12 major proteins found in the female salivary glands and each morphological region of the female glands contained different major proteins. Two-dimensional gel electrophoresis showed approximately 20 major and several minor protein spots displaying relative molecular masses from 10 to 72 kDa with electric points ranging from 3.9 to 10. At least 15 glycoproteins were detected in the female glands. Similar electrophoretic protein profiles were detected comparing the male and proximal-lateral lobes of the female glands, suggesting that these lobes are responsible for sugar feeding. Blood-feeding proteins, i.e., putative 5'-nucleotidase/apyrase, anti-platelet protein, long-form D7 salivary protein, D7-related 1 protein, and gSG6, were detected in the distal-lateral lobes (DL) and/or medial lobes (ML) of the female glands. The major spots related to housekeeping proteins from other arthropod species including Culex quinquefasciatus serine/threonine-protein kinase rio3 expressed in both male and female glands, Ixodes scapularis putative sil1 expressed in DL and ML, and I. scapularis putative cyclophilin A expressed in DL. These results provide information for further study on the salivary gland proteins of A. campestris-like that are involved in hematophagy and disease transmission.

U2 - 10.1007/s00436-012-3233-y

DO - 10.1007/s00436-012-3233-y

M3 - Journal article

C2 - 23263250

VL - 112

SP - 1065

EP - 1075

JO - Parasitology Research

JF - Parasitology Research

SN - 0044-3255

IS - 3

ER -