Analysis of the interaction of an anti-HIV peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), with gp 120 and CD4 by surface plasmon resonance

Tamamura, Hirokazu; Ishihara, Tsunehito; Otaka, Akira; Murakami, Tsutomu; Ibuka, Toshiro; Waki, Michinori; Matsumoto, Aki; Yamamoto, Naoki; Fujii, Nobutaka

doi:10.1016/s0167-4838(96)00113-6

Cited by 26 publications

(8 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Even though the mechanism involved has not been elucidated, the authors suggested that the biochemical properties of IL-26 may be responsible, at least in part, for the protective activity of IL-26. This hypothesis is supported by previous studies showing that AMP can prevent virus infectivity by (i) causing virus membrane instability, rendering them unable to infect host cells (68, 69), or (ii) by interfering with the virus binding to host cells (through interaction with binding structures of the virus or with receptors at the surface of target cells) (70–72). A role for IL-26 in antiviral defense is also supported by its overexpression in the embryonic zebra fish cell line ZF4 infected by the aquatic Birnavirus Infectious pancreatic necrosis virus (73).…”

Section: Biological Properties Of Il-26supporting

confidence: 63%

IL-26, a Cytokine With Roles in Extracellular DNA-Induced Inflammation and Microbial Defense

et al. 2019

View full text Add to dashboard Cite

Interleukin 26 (IL-26) is the most recently identified member of the IL-20 cytokine subfamily, and is a novel mediator of inflammation overexpressed in activated or transformed T cells. Novel properties have recently been assigned to IL-26, owing to its non-conventional cationic, and amphipathic features. IL-26 binds to DNA released from damaged cells and, as a carrier molecule for extracellular DNA, links DNA to inflammation. This observation suggests that IL-26 may act both as a driver and an effector of inflammation, leading to the establishment of a deleterious amplification loop and, ultimately, sustained inflammation. Thus, IL-26 emerges as an important mediator in local immunity/inflammation. The dysregulated expression and extracellular DNA carrier capacity of IL-26 may have profound consequences for the chronicity of inflammation. IL-26 also exhibits direct antimicrobial properties. This review summarizes recent advances on the biology of IL-26 and discusses its roles as a novel kinocidin.

show abstract

Section: Biological Properties Of Il-26supporting

confidence: 63%

IL-26, a Cytokine With Roles in Extracellular DNA-Induced Inflammation and Microbial Defense

et al. 2019

View full text Add to dashboard Cite

show abstract

“…Unlike T22, retrocyclin-1 protected against both T-tropic and M-tropic HIV-1 strains. In addition, retrocyclin-1 bound gp120 and CD4 with three-to fivefold higher affinity than did T22, whose K D values for gp120 and CD4 were 167 nM and 101 nM, respectively (41,42).…”

Section: Discussionmentioning

confidence: 92%

Retrocyclin, an Antiretroviral θ-Defensin, Is a Lectin

Wang¹,

Cole²,

Hong³

et al. 2003

The Journal of Immunology

183

164

View full text Add to dashboard Cite

θ-Defensins are circular octadecapeptides that contain an internal tridisulfide ladder. Because retrocyclin-1, an ancestral hominid θ-defensin, can protect human cells in vitro from infection by T- and M-tropic strains of HIV-1, we used surface plasmon resonance techniques to study its binding to glycoproteins and glycolipids implicated in HIV-1 entry. Retrocyclin-1 bound with high affinity to gp120 (Kd, 35.4 nM), CD4 (Kd, 31 nM), and galactosylceramide (Kd, 24.1 nM). Neither a circular form of retrocyclin without its tridisulfide ladder nor its β-hairpin precursor with these disulfides intact bound gp120 or CD4 effectively. Retrocyclin also bound fetuin, an extensively glycosylated protein, with high affinity, but it did not bind nonglycosylated gp120 or BSA. However, retrocyclin did bind to a neoglycoprotein, BSA, with covalently attached sugar residues. Experiments with glycosidase-treated fetuin, gp120, and CD4 revealed that both O-linked and N-linked sugars were used as binding sites. In a panel of retrocyclin variants, binding to immobilized gp120 and CD4 were highly correlated to each other and to the peptide’s ability to protect human PBMCs from infection by HIV-1. Although small, cysteine-rich antimicrobial peptides with lectin-like properties exist in plants, θ-defensins are the first such molecules to be identified in vertebrates. Retrocyclin’s ability to recognize and bind carbohydrate-containing surface molecules is integrally related to its ability to protect cells from HIV-1 infection.

show abstract

“…Antimicrobial peptides might interact directly with specific viral receptors on the host cell (42,240), influencing viral attachment, entry, or intracellular shuttling. The most obvious example of this is the known ability of the polyphemusin analogue T22 to bind to the chemokine receptor CXCR4, which serves as a coreceptor for HIV-1 entry into T cells (173,243).…”

Section: Mode Of Action Of Antiviral Peptidesmentioning

confidence: 99%

Peptide Antimicrobial Agents

2006

View full text Add to dashboard Cite

SUMMARY Antimicrobial host defense peptides are produced by all complex organisms as well as some microbes and have diverse and complex antimicrobial activities. Collectively these peptides demonstrate a broad range of antiviral and antibacterial activities and modes of action, and it is important to distinguish between direct microbicidal and indirect activities against such pathogens. The structural requirements of peptides for antiviral and antibacterial activities are evaluated in light of the diverse set of primary and secondary structures described for host defense peptides. Peptides with antifungal and antiparasitic activities are discussed in less detail, although the broad-spectrum activities of such peptides indicate that they are important host defense molecules. Knowledge regarding the relationship between peptide structure and function as well as their mechanism of action is being applied in the design of antimicrobial peptide variants as potential novel therapeutic agents.

show abstract

Analysis of the interaction of an anti-HIV peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), with gp 120 and CD4 by surface plasmon resonance

Cited by 26 publications

References 21 publications

IL-26, a Cytokine With Roles in Extracellular DNA-Induced Inflammation and Microbial Defense

IL-26, a Cytokine With Roles in Extracellular DNA-Induced Inflammation and Microbial Defense

Retrocyclin, an Antiretroviral θ-Defensin, Is a Lectin

Peptide Antimicrobial Agents

Contact Info

Product

Resources

About