Investigation the Possibility of Using Peptides with a Helical Repeating Pattern of Hydro-Phobic and Hydrophilic Residues to Inhibit IL-10

Guoying Ni; Shu Chen; Yuedong Yang; Scott F Cummins; Jian Zhan; Zhixiu Li; Bin Zhu; Kate Mounsey; Shelley Walton; Ming Q Wei; Yuejian Wang; Yaoqi Zhou; Tianfang Wang; Xiaosong Liu

doi:10.1371/journal.pone.0153939

Investigation the Possibility of Using Peptides with a Helical Repeating Pattern of Hydro-Phobic and Hydrophilic Residues to Inhibit IL-10

PLoS One. 2016 Apr 21;11(4):e0153939. doi: 10.1371/journal.pone.0153939. eCollection 2016.

Authors

Guoying Ni^{1

2}, Shu Chen³, Yuedong Yang⁴, Scott F Cummins¹, Jian Zhan⁴, Zhixiu Li⁵, Bin Zhu³, Kate Mounsey⁶, Shelley Walton⁶, Ming Q Wei², Yuejian Wang³, Yaoqi Zhou⁴, Tianfang Wang¹, Xiaosong Liu^{1

3}

Affiliations

¹ Genecology Research Centre, University of the Sunshine Coast, Maroochydore DC, Australia.
² School of Medical Science, Griffith Health Institute, Griffith University, Gold Coast, Australia.
³ Cancer Research Institute, Foshan First People's Hospital, Foshan, Guangdong, China.
⁴ The Institute for Glycomics and School of Information and Communication Technology, Griffith University, Gold Coast, Australia.
⁵ Diamantina Institute, University of Queensland, Woolloongabba, Australia.
⁶ Inflammation and Healing Research Cluster, School of Health and Sport Sciences, University of Sunshine Coast, Maroochydore DC, Australia.

Abstract

Blockade of IL-10 signalling clears chronic viral and bacterial infections. Immunization together with blockade of IL-10 signalling or relatively low level of IL-10 further enhances viral and bacterial clearance. IL-10 functions through binding to interleukin 10 receptor (IL-10R). Here we showed that peptides P1 and P2 with the hydrophobic and hydrophilic pattern of the IL10R-binding helix in IL-10 could bind with either IL-10R1 or IL-10, and inhibit inflammatory signals with long duration and negligible cytotoxicity in vitro. Furthermore, P2 can enhance antigen specific CD8+ T cell responses in mice induced by the vaccine based on a long peptide of protein E7 in a human papillomavirus type 16.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Female
Human papillomavirus 16 / immunology
Humans
Immunization
Interleukin-10 / antagonists & inhibitors*
Interleukin-10 / immunology
Mice
Mice, Inbred C57BL
Molecular Sequence Data
Papillomavirus E7 Proteins / genetics
Papillomavirus E7 Proteins / immunology*
Papillomavirus Infections / immunology*
Papillomavirus Infections / metabolism
Papillomavirus Infections / prevention & control*
Papillomavirus Infections / virology
Papillomavirus Vaccines / immunology*
Protein Conformation
Sequence Homology, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Surface Plasmon Resonance
Vaccines, Subunit / chemistry*
Vaccines, Subunit / immunology
Vaccines, Subunit / pharmacology*

Substances

IL10 protein, human
Papillomavirus E7 Proteins
Papillomavirus Vaccines
Vaccines, Subunit
oncogene protein E7, Human papillomavirus type 16
Interleukin-10

Grants and funding

Support was provided by the National Natural Science Foundation of China (www.nsfc.gov.cn/publish/portal1/), 81472451 to XL and TW; and the National Health and Medical Research Council of Australia (www.nhmrc.gov.au), 1059775 to YZ. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.