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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
.
Abstract
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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