跳至主要内容

The HPV L1 C-terminal conserved sequence polypeptide|EVNLKEKFSADLDQFPLGRKFLLQAGLKAK

文献作者:Le Wang, Yu-Chang Hu, Chang-Yi Xiao, Fei Wang, Yu-Fei Liu, Li-Hua Tang, Rong-Shuang Xiao   《Journal of Virological Methods》


ABSTRACTS

AIMS

To determine the value of a monoclonal antibody panel against a C-terminal conserved sequence polypeptide of human papillomavirus (HPV) L1 (a major capsid protein) for the detection of HPV in cervical exfoliated cells, as well as the potential of this antibody panel to be developed into an assay kit for the clinical screening of cervical cancer.

METHODS

Cervical exfoliated cells were collected at a gynecology clinic. One part of each sample was sent to the Department of Pathology for HPV genotyping, and the other part was sent to the Department of Pathology for cytologic testing and then to the laboratory for immunological histological chemistry (IHC) assay in which an HPV L1 C-terminal conserved sequence polypeptide-induced mouse monoclonal antibody panel was used to detect HPV L1.

RESULTS

Cervical cell samples were collected from 514 patients at the gynecology clinic; of these, 339 samples were sent for HPV genotyping, and 220 were HPV positive (64.90%, 220/339). Moreover, the duplicate samples from these 339 patients were sent for IHC assay, and 229 samples were positive (67.55%, 229/339). The IHC result was concordant with that obtained by HPV genotyping

CONCLUSION

This study showed that use of the HPV L1 C-terminal conserved sequence polypeptide-induced mouse monoclonal antibody panel was of great value for the detection of HPV in cervical cells; the resulting detection rate was comparable to that obtained using the commercial HPV genotyping kit that is currently in use in clinical practice.
KEY WORDS
Human papillomavirus; Major capsid protein; Monoclonal antibody; Immunological histochemistry; Cervical exfoliated cells
SCREENSHOT

RELATED PRODUCTS
The HPV L1 C-terminal conserved sequence polypeptide (30 amino acids: EVNLKEKFSADLDQFPLGRKFLLQAGLKAK) was synthesized by ChinaPeptides Co., Ltd.
CHAINING
https://www.sciencedirect.com/science/article/pii/S0166093417305773
Number of Residues:30
1-Letter Code:EVNLKEKFSADLDQFPLGRKFLLQAGLKAK
3-Letter Code:Glu-Val-Asn-Leu-Lys-Glu-Lys-Phe-Ser-Ala-Asp-Leu-Asp-Gln-Phe-Pro-Leu-Gly-Arg-Lys-Phe-Leu-Leu-Gln-Ala-Gly-Leu-Lys-Ala-Lys

Molecular weight (Mr):3405 g/mol
Isoelectric point:10.0
Net charge at pH 7.0:2.0
Average hydrophilicity:0.3
Ratio of hydrophilic residues / total number of residues:47 %

评论

此博客中的热门博文

The Catalytically Inactive Mutation of the Ubiquitin-Conjugating Enzyme CDC34 Affects its Stability and Cell Proliferation

Author:Xun Liu, Yang Zhang, Zhanhong Hu, Qian Li, Lu Yang,  Guoqiang Xu     《The Protein Journal》 ABSTRACTS The ubiquitin proteasome system (UPS) plays important roles in the regulation of protein stability, localization, and activity. A myriad of studies have focused on the functions of ubiquitin ligases E3s and deubiquitinating enzymes DUBs due to their specificity in the recognition of downstream substrates. However, the roles of the most ubiquitin-conjugating enzymes E2s are not completely understood except that they transport the activated ubiquitin and form E2–E3 protein complexes. Ubiquitin-conjugating enzyme CDC34 can promote the degradation of downstream targets through the UPS whereas its non-catalytic functions are still elusive. Here, we find that mutation of the catalytically active cysteine to serine (C93S) results in the reduced ubiquitination, increased stability, and attenuated degradation rate of CDC34. Through semi-quantitative proteom...

Identification and Inhibitory Mechanism of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Bovine Hemoglobin

Author:Ying Wang, Yiqun Jiang, Yongguang Yin, Jiyun Liu,  Long Ding, Jingbo Liu, Ting Zhang     《The Protein Journal》 ABSTRACTS Angiotensin I-converting enzyme (ACE, EC.3.4.15.1) inhibitory peptide is an efficacious therapy for hypertension. In this study, four dipeptides, TY, FD, FL and FG, were identified from the desalted fraction of bovine hemoglobin hydrolysate, obtained by in vitro simulated gastrointestinal digestion, via liquid chromatography-tandem mass spectrometry (LC-MS/MS). The IC 50   value of TY and FL are 96.43?±?6.17 and 290.66?±?57.92  μM, respectively. The result of molecular docking indicated that TY occupied the ACE subsite S1 and S1′ with a lowest estimated binding energy of ?9.96  Kcal/mol, while FL occupied the subsite S5 with a lowest estimated binding energy of ?9.37  Kcal/mol. The subsite S1′ and S2′ are closer to the ACE active center (Zn 2+ ) than S5, and the lowest estimated binding energy of TY is lower ...

Preparation of an antimicrobial surface by direct assembly of antimicrobial peptide with its surface binding activity

Author:Junjian Chen, Yuchen Zhu, Yancheng Song, Lin Wang,  Jiezhao Zhan, Jingcai He, Jian Zheng, Chunting Zhong, Xuetao Shi, Sa Liu, Li Ren and Yingjun Wang     《Journal of Materials Chemistry B》 ABSTRACTS Antimicrobial peptides (AMPs) are a broad prospect for clinical application against bacterial infections of biomaterials. However, a bottleneck exists as there is a lack of simple technology to prepare AMPs on biomaterials with sufficient activity, as the activity of AMP is dependent on the correct orientation on the biomaterial. In the present study, based on the conventional AMP (Tet213: KRWWKWWRRC) and surface binding peptide (SKHKGGKHKGGKHKG), we designed an Anchor-AMP that could be directly assembled onto the surface of the biomaterial and also showed excellent antimicrobial activity. By characterizing the surface using a quartz crystal microbalance with dissipation (QCM-D), contact angle, atom force microscopy (AFM) and X-ray photoelectron spectr...