Glycoprotein E (gE) of HSV plays a key role in cell-to-cell spread and virus-induced cell fusion. Here, we report that this function of gE requires the cooperation of tegument proteins UL11, UL16, and UL21. We found that the four proteins come together with very high efficiency to form a complex in transfected cells and in a manner that is regulated and coordinated. In particular, the inefficient interaction of UL16 with each membrane protein (UL11 and gE) observed in pairwise transfections became efficient when other binding partners were present. The significance of these interactions was revealed in studies of viral mutants, which showed that each of these tegument proteins is critical for processing, transport, and biological activity of gE. These findings provide insights into the mechanisms of how gE executes its function and also have implications in understanding HSV assembly and budding.
UL16 is a tegument protein of herpes simplex virus (HSV) that is conserved among all members of the Herpesviridae, but its function is poorly understood. Previous studies revealed that UL16 is associated with capsids in the cytoplasm and interacts with the membrane protein UL11, which suggested a "bridging" function during cytoplasmic envelopment, but this conjecture has not been tested. To gain further insight, cells infected with UL16-null mutants were examined by electron microscopy. No defects in the transport of capsids to cytoplasmic membranes were observed, but the wrapping of capsids with membranes was delayed. Moreover, clusters of cytoplasmic capsids were often observed, but only near membranes, where they were wrapped to produce multiple capsids within a single envelope. Normal virion production was restored when UL16 was expressed either by complementing cells or from a novel position in the HSV genome. When the composition of the UL16-null viruses was analyzed, a reduction in the packaging of glycoprotein E (gE) was observed, which was not surprising, since it has been reported that UL16 interacts with this glycoprotein. However, levels of the tegument protein VP22 were also dramatically reduced in virions, even though this gE-binding protein has been shown not to depend on its membrane partner for packaging. Cotransfection experiments revealed that UL16 and VP22 can interact in the absence of other viral proteins. These results extend the UL16 interaction network beyond its previously identified binding partners to include VP22 and provide evidence that UL16 plays an important function at the membrane during virion production. Infectious herpesviruses contain approximately 40 viral proteins and are produced when their DNA-containing capsids are wrapped with a cell-derived membrane in the cytoplasm (1). This envelopment process is driven by complex interactions that are still poorly understood but is known to involve bridging interactions provided by a growing list of tegument proteins, which provide linkages between the capsid and viral membrane proteins (1-3). The UL16 tegument protein of herpes simplex virus (HSV) is remarkable for its numerous interactions with several other viral proteins, namely, tegument protein UL21 (4, 5), membrane protein UL11 (4, 6-8), membrane glycoprotein E (gE) (4, 9), and an unidentified protein(s) that is associated with the capsid (10-12). UL16 is conserved among all the alpha-, beta-, and gammaherpesvirinae (2, 13, 14), but its actual function remains unknown.There are several reasons for suggesting a role for UL16 in HSV envelopment. The earliest study showed that a U L 16-null mutant (here named the ⌬U L 16B mutant) produces infectious virions at a level only one-tenth that of the wild-type virus (15). Also, UL16 has been shown to be bound in some manner to cytoplasmic capsids (10, 16, 17), and thus, its direct interactions with membrane proteins UL11 (8) and gE (9) suggest that UL16 might provide bridging functions that help drive virion production, as first pro...
A pathogenesis related protein (AhPR10) is identified from a clone of 6-day old Arachis hypogaea L. (peanut) cDNA library. The clone expressed as a approximately 20 kDa protein in E. coli. Nucleotide sequence derived amino acid sequence of the coding region shows its homology with PR10 proteins having Betv1 domain and P loop motif. Recombinant AhPR10 has ribonuclease activity, and antifungal activity against the peanut pathogens Fusarium oxysporum and Rhizoctonia solani. Mutant protein AhPR10-K54N where lys54 is mutated to asn54 loses its ribonuclease and antifungal activities. FITC labeled AhPR10 and AhPR10-K54N are internalized by hyphae of F. oxysporum and R. solani but the later protein does not inhibit the fungal growth. This suggests that the ribonuclease function of AhPR10 is essential for its antifungal activity. Energy and temperature dependent internalization of AhPR10 into sensitive fungal hyphae indicate that internalization of the protein occurs through active uptake.
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