B-cell epitope peptide vaccination targeting dimer interface of epidermal growth factor receptor (EGFR).

Epidermal growth factor receptor (EGFR) was the first receptor to be proposed as the target for cancer therapy, however, the anti-EGFR therapy showed a low response rate clinically. Dimerization plays a key role in the activation of EGFR, so targeting the conservative dimer interface probably improve the responses of anti-EGFR clinically. To evoke a high titers of antibodies (Abs) targeting the dimer interface of EGFR in patients, a chimeric peptide, comprising a linear B-cell epitope peptide from the highly conservative β-hairpin loop of dimer interface of human EGFR (EGFR237-267) and a 'promiscuous' Th-cell epitope MVF from the measles virus fusion protein, was constructed.

[Construction and immunogenicity analysis of tumor peptide vaccine P64k-EGFR(262-328); targeting the dimmerization interface of EGFR].

Objective: To construct a tumor-specific peptide vaccine P64k-EGFR(262-328); targeting the dimerization interface of EGFR and analyze its immunogenicity in BALB/c mice.

Methods: The fusion gene of P64k-EGFR(262-328); was amplified by splicing overlap extension-PCR (SOE-PCR) and cloned into the pMD18-T vector. After double-enzyme cleavage and sequence analysis, the fusion gene was cloned into the expression vector pET-21b by digestion with Nde I and Hind III and then transformed into the BL21(DE3).

Expression and purification of chimeric peptide comprising EGFR B-cell epitope and measles virus fusion protein T-cell epitope in Escherichia coli.

Chimeric peptide MVF-EGFR(237-267), comprising a B-cell epitope from the dimerization interface of human epidermal growth factor receptor (EGFR) and a promiscuous T-cell epitope from measles virus fusion protein (MVF), is a promising candidate antigen peptide for therapeutic vaccine. To establish a high-efficiency preparation process of this small peptide, the coding sequence was cloned into pET-21b and pET-32a respectively, to be expressed alone or in the form of fusion protein with thioredoxin (Trx) and His(6)-tag in Escherichia coli BL21 (DE3). The chimeric peptide failed to be expressed alone, but over-expressed in the fusion form, which presented as soluble protein and took up more than 30% of total proteins of host cells.

[Clinical factors relating to the arterial elastic function measured by PWV, C1/C2 and AI in hypertensive patients].

Objective: To analyze the clinical factors relating to arterial elastic function measured with pulse wave velocity (PWV), large and small arterial elastic indexes (C(1) and C(2)) and augmentation index (AI) in hypertensive patients.

Methods: A total of 2176 hypertensive patients were enrolled and divided into three groups: Elastic function was measured in 1100 subjects by (PWV), in 647 subjects by C(1) and C(2) and in 429 by AI.

Results: PWV was positively correlated with age, systolic pressure, pulse pressure and negatively correlated with body height and weights (all P < 0.