Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococca
To our best knowledge, all of the fungal immunomodulatory proteins (FIPs) have been successfully extracted and identified in Basidomycetes, with only the exception of FIP from ascomycete Nectria haematococca (FIP-nha) discovered through homology alignment most recently. In this work, a gene encoding...
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MDPI AG
2014-09-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | http://www.mdpi.com/1422-0067/15/10/17751 |
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| author | Shuying Li Ying Nie Yang Ding Lijun Shi Xuanming Tang |
| author_facet | Shuying Li Ying Nie Yang Ding Lijun Shi Xuanming Tang |
| author_sort | Shuying Li |
| collection | DOAJ |
| description | To our best knowledge, all of the fungal immunomodulatory proteins (FIPs) have been successfully extracted and identified in Basidomycetes, with only the exception of FIP from ascomycete Nectria haematococca (FIP-nha) discovered through homology alignment most recently. In this work, a gene encoding FIP-nha was synthesized and recombinantly expressed in an Escherichia coli expression system. SDS-PAGE and MALDI-MS analyses of recombinant FIP-nha (rFIP-nha) indicated that the gene was successfully expressed. The yield of the bioactive FIP-nha protein was 42.7 mg/L. In vitro assays of biological activity indicated that the rFIP-nha caused hemagglutination of human and rabbit red blood cells, significantly stimulated mouse spleen lymphocyte proliferation, and enhanced expression of interleukin-2 (IL-2) released from mouse splenocytes, revealing a strong antitumor effect against HL60, HepG2 and MGC823. Through this work, we constructed a rapid and efficient method of FIP production, and suggested that FIP-nha is a valuable candidate for use in future medical care and pharmaceutical products. |
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| language | English |
| last_indexed | 2024-04-12T00:32:08Z |
| publishDate | 2014-09-01 |
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| spelling | doaj.art-78ac637214e24cb2afc8eefbe54e17622022-12-22T03:55:18ZengMDPI AGInternational Journal of Molecular Sciences1422-00672014-09-011510177511776410.3390/ijms151017751ijms151017751Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococcaShuying Li0Ying Nie1Yang Ding2Lijun Shi3Xuanming Tang4Institute of Agro-products Processing Science and Technology, Chinese Academy of Agricultural Sciences (CAAS), Key Laboratory of Agro-products Processing, Ministry of Agriculture, No. 2 Yuan Ming Yuan West Road, Beijing 100193, ChinaInstitute of Agro-products Processing Science and Technology, Chinese Academy of Agricultural Sciences (CAAS), Key Laboratory of Agro-products Processing, Ministry of Agriculture, No. 2 Yuan Ming Yuan West Road, Beijing 100193, ChinaInstitute of Agro-products Processing Science and Technology, Chinese Academy of Agricultural Sciences (CAAS), Key Laboratory of Agro-products Processing, Ministry of Agriculture, No. 2 Yuan Ming Yuan West Road, Beijing 100193, ChinaInstitute of Animal Science and Veterinary Medicine, CAAS, No. 2 Yuan Ming Yuan West Road, Beijing 100193, ChinaInstitute of Agro-products Processing Science and Technology, Chinese Academy of Agricultural Sciences (CAAS), Key Laboratory of Agro-products Processing, Ministry of Agriculture, No. 2 Yuan Ming Yuan West Road, Beijing 100193, ChinaTo our best knowledge, all of the fungal immunomodulatory proteins (FIPs) have been successfully extracted and identified in Basidomycetes, with only the exception of FIP from ascomycete Nectria haematococca (FIP-nha) discovered through homology alignment most recently. In this work, a gene encoding FIP-nha was synthesized and recombinantly expressed in an Escherichia coli expression system. SDS-PAGE and MALDI-MS analyses of recombinant FIP-nha (rFIP-nha) indicated that the gene was successfully expressed. The yield of the bioactive FIP-nha protein was 42.7 mg/L. In vitro assays of biological activity indicated that the rFIP-nha caused hemagglutination of human and rabbit red blood cells, significantly stimulated mouse spleen lymphocyte proliferation, and enhanced expression of interleukin-2 (IL-2) released from mouse splenocytes, revealing a strong antitumor effect against HL60, HepG2 and MGC823. Through this work, we constructed a rapid and efficient method of FIP production, and suggested that FIP-nha is a valuable candidate for use in future medical care and pharmaceutical products.http://www.mdpi.com/1422-0067/15/10/17751antitumorfungal immunomodulatory protein (FIP)hemagglutinationinterleukin-2 (IL-2)Nectria haematococcaproliferation |
| spellingShingle | Shuying Li Ying Nie Yang Ding Lijun Shi Xuanming Tang Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococca International Journal of Molecular Sciences antitumor fungal immunomodulatory protein (FIP) hemagglutination interleukin-2 (IL-2) Nectria haematococca proliferation |
| title | Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococca |
| title_full | Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococca |
| title_fullStr | Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococca |
| title_full_unstemmed | Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococca |
| title_short | Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococca |
| title_sort | recombinant expression of a novel fungal immunomodulatory protein with human tumor cell antiproliferative activity from nectria haematococca |
| topic | antitumor fungal immunomodulatory protein (FIP) hemagglutination interleukin-2 (IL-2) Nectria haematococca proliferation |
| url | http://www.mdpi.com/1422-0067/15/10/17751 |
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