Proteomic profiles of soluble proteins from the esophageal gland in female Meloidogyne incognita

• Published in: International journal for parasitology Vol. 42; no. 13-14; pp. 1177 - 1183
• Main Authors: Wang, Xin-Rong, Moreno, Yovany A., Wu, Han-Rong, Ma, Chao, Li, Yun-feng, Zhang, Jin-ai, Yang, Chong, Sun, Si, Ma, Wei-jie, Geary, Timothy G.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01-12-2012; Elsevier
• Subjects: Animals; Biological and medical sciences; Esophageal gland cells; Esophagus - metabolism; Female; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation - physiology; Helminth Proteins - genetics; Helminth Proteins - metabolism; Invertebrates; LC–MS/MS; Life cycle. Host-agent relationship. Pathogenesis; Meloidogyne incognita; Nemathelminthia. Plathelmintha; Nematode; Plant parasite; Protein extraction; Proteomics; Protozoa; Secretome; Transcriptome; Tylenchoidea - anatomy & histology; Tylenchoidea - metabolism; Meloidogyne incognita; Protein extraction; Plant parasite; Nematode; Secretome; LC–MS/MS; Esophageal gland cells; Parasite; Gland; Protein; LC-MS/MS; Phytophagous; Helmintha; Female; Nemathelminthia; Invertebrata; Nematoda
• ISSN: 0020-7519; 1879-0135
• DOI: 10.1016/j.ijpara.2012.10.008

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► A novel method was used to collect proteins secreted by adult female Meloidogyne incognita. ► The identification of the proteins in this compartment was accomplished by standard MS/MS proteomics analyses. ► ‘Secretomes’ of adults and larvae differ, suggesting stage-specific roles in infection and feeding site maintenance.
Meloidogyne incognita can infect multiple plant species. Proteins synthesized in the esophageal glands and secreted through the stylet of plant parasitic nematodes play critical roles in the plant-nematode interactions. Female M. incognita live for approximately 15days, embedded in a host plant, but their esophageal gland proteins have not yet been comprehensively analyzed. In this study, a new bacterium-contamination-resistant method for collecting soluble proteins from esophageal gland cells (SPEGC) of female M. incognita was established. Approximately 5μg of freeze-dried proteins could be extracted from 150 female M. incognita. Bands of a one-dimensional SDS–polyacrylamide gel were excised after electrophoresis of 20μg of protein and were analyzed. Two hundred and forty-six proteins from SPEGC of female M. incognita were identified by LC–MS/MS. Gene Ontology analysis suggests that many of the secreted proteins are involved in protein or carbohydrate metabolism and proteolysis. Some of the SPEGC (46.3%) were predicted to be secreted through classical or non-classical secretory pathways. The described method presents a new approach for the identification of proteins stored in SPEGC of an important plant parasitic nematode. This global proteomic profile of SPEGC provides a basis for future studies to elucidate the functions of proteins secreted from female M. incognita on plant responses.