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Int J Mol Sci
2014 Sep 30;1510:17751-64. doi: 10.3390/ijms151017751.
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Recombinant expression of a novel fungal immunomodulatory protein with human tumor cell antiproliferative activity from Nectria haematococca.
Li S
,
Nie Y
,
Ding Y
,
Shi L
,
Tang X
.
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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.
Figure 1. Purification and identification of rFIP-nha. (A) Tricine-SDS-PAGE analysis. GST-FIP-nha was purified using a GST column, digested with thrombin and eluted with PBS and glutathione. Lane 1: Eluate with PBS. Lanes 2 and 3: Eluates with glutathione. Lane 4: Standard protein molecular weight markers. Arrows 1, 2, and 3 indicated the purified rFIP-nha, GST, and GST-FIP-nha, respectively; (B) Amino acid sequence of deduced FIP-nha. Nine peptide fragments consisting of 91 residues identified by MALDI-MS are underlined.
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