The pathway of infection of Autographa californica nuclear polyhedrosis virus in an insect host

An immunohistochemical study was conducted to detect the temporal infection sequence of Autographa californica M nuclear polyhedrosis virus in Trichoplusia ni larvae. Staining patterns indicated that the initial infection occurred in the midgut, simultaneously in columnar epithelial and regenerative cells, but that subsequently this tissue recovered. A major envelope glycoprotein stained in a polar fashion when it was expressed in columnar epithelial cells, but not when expressed in other cells types. Systemic infection was mediated by free virus for some tissues whereas infected hemocytes appeared to spread virus to other tissues by an unknown mechanism. A cell to cell spread within several tissues was detected. These results have important implications for baculoviruses engineered for improving their pesticide potential.     

A mammalian thioglycosidase

A thioglycosidase capable of catalyzing the hydrolysis of 6-purine beta-d-glucothiopyranoside and other thioglycosides has been found in a number of mammalian tissues (including tumors) as well as in almond emulsin. The substrate specificity of mammalian thioglycosidase involves both the aglycone and the glycosyl moieties.     

Interferon action: RNA cleavage pattern of a (2'-5')oligoadenylate--dependent endonuclease

One of the mediators of interferon action is a latent endoribonuclease (ribonuclease L) that is activated by (2'-5')oligoadenylates. Among the homopolymers of the four common ribonucleotides, activated ribonuclease L degrades at an appreciable rate only polyuridylic acid. In two natural RNA's tested the most frequent ribonuclease L cleavages occur after UA, UG, and UU (A, adenine; U, uracil; and G, guanine) and much less frequent cleavages after CA and AC (C, cytosine).