CAP37-Derived Antimicrobial Peptides Have In Vitro Antiviral Activity against Adenovirus and Herpes Simplex Virus Type 1

被引：10

作者：

Gordon, Y. Jerold ^{[1
]}

Romanowski, Eric G.

Shanks, Robert M. Q.

Yates, Kathleen A.

Hinsley, Heather ^{[2
]}

Pereira, H. Anne ^{[2
]}

机构：

[1] Univ Pittsburgh, Inst Eye & Ear, Charles T Campbell Lab,Dept Ophthalmol,Sch Med, Ophthalm Microbiol Lab,UPMC Eye Ctr,OVSRC, Pittsburgh, PA 15213 USA

[2] Univ Oklahoma, Hlth Sci Ctr, Dept Pathol, Oklahoma City, OK USA

来源：

CURRENT EYE RESEARCH | 2009年 / 34卷 / 03期

关键词：

adenovirus; antimicrobial peptide; azurocidin; CAP37; herpes simplex virus; INFLAMMATORY MEDIATOR; ALPHA-DEFENSIN; EXPRESSION; CAP37; NEUTROPHILS; AZUROCIDIN; PROTEINS; MONOCYTE; BINDING; MODULATION;

D O I：

10.1080/02713680802714066

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

Purpose: The antiviral activity of an established antibacterial CAP37 domain and its extracellular mechanism of action were investigated. Methods: CAP37-derived peptides modified to assess the importance of disulfide bonds were evaluated in cytotoxicity and antiviral assays (direct time kill, dose dependency, and TOTO-1) for adenovirus (Ad) and herpes simplex virus type 1 (HSV-1). Results: Variable virus, adenovirus serotype-dependent, and dose-dependent inhibition were demonstrated without cytotoxicity. For peptide A (CAP3720-44), TOTO-1 dye uptake was demonstrated for Ad5 and HSV-1. Conclusions: Unlike the antibacterial activity of this CAP37 domain, its antiviral activity is not fully dependent upon disulfide bond formation. Viral inhibition appears to result, in part, from disruption of the envelope and/or capsid.

引用

页码：241 / 249

页数：9

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