<span style="color:black;mso-bidi-language:HI">Po<span style="color:#121212; mso-bidi-language:HI">s<span style="color:black;mso-bidi-language:HI">sible mechanism of action of anti<span style="color:#282828;mso-bidi-language: HI">v<span style="color:black;mso-bidi-language:HI">iral pr<span style="color:#121212;mso-bidi-language:HI">o<span style="color:black; mso-bidi-language:HI">teins fr<span style="color:#121212;mso-bidi-language: HI">o<span style="color:black;mso-bidi-language:HI">m th<span style="color:#121212;mso-bidi-language:HI">e <span style="color:black; mso-bidi-language:HI">l<span style="color:#282828;mso-bidi-language: HI">e<span style="color:black;mso-bidi-language:HI">a<span style="color:#282828;mso-bidi-language:HI">v<span style="color:black; mso-bidi-language:HI">es of <i><span style="color:#121212;mso-bidi-language:HI">C</span></i><i><span style="color:black;mso-bidi-language:HI">henopodium album </span></i><span style="mso-bidi-font-family:Arial;color:black;mso-bidi-language:HI">L. </span></span></span></span></span></span></span></span></span></span></span></span></span></span></span></span>

Abstract

<span style="mso-bidi-font-family:Arial;mso-bidi-language:HI">Antiviral Protiens (AVPs) named CAP-I and CAP-II purified from the leaves of <i>Chenopodium album cv</i> Pusa Bathura-1 indaced systemic against tobacco mosaic virus (TMV) and sunnhemp rosette virus (SRV) in both hypersenstitive as well as systemic hosts. An increased accumulation of two polypeptides (~17 kDa and ~26 kDa) was observed in untreated upper leaves of <i>Cyamopsis tetragonoloba</i> plants whose basal leaves were treated with CAP-I/CAP-II. Both AVPs exhibited ribosomal RNA N-glycosidase activity on 28S rRNA of tobacco leaves and also caused <i>in vitro</i> degradation of TMV RNA. It is suggested that the CAP-I and –II are multi-functional and may be acting at multiple levels to ensure maximum possible inhibition of viral infection.

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