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Sex Transm Infect. 2002 Jun;78(3):219-21.
The evolution of sexually transmitted infections in the Ukraine.

Mavrov GI, Bondarenko GM.

Institute of Dermatology and Venereology, Kharkiv, Ukraine. uniidilink.kharkov.ua

OBJECTIVES: To evaluate trends in the national and regional reporting of syphilis, gonorrhoea, chlamydia, genital herpes, trichomoniasis, and HIV in Ukraine. METHODS: Annual notification rates of infection per 10(5) population in three regions of Ukraine--Donetsk, Mikolaiv, Chernivtsi--and also among children, adolescents, and pregnant women were used as indicators for the spread of sexually transmitted infections (STIs) in the Ukraine from 1994 to 2000. The estimates were based on a review of medical literature, reported data from STD clinics, and local epidemiological surveys. An analysis of the trends was made. RESULTS: The notification rate of trichomoniasis rose from 284.3 in 1997 to 330.8 in 2000. The same for syphilis was 68.7 per 100,000 population in 1994 peaked in 1996 with 150.9 falling to 91.5 in 2000. The reported incidence of gonorrhoea has been falling recently to 52.7/10(5) in 2000 (a 104.6% decrease since 1994). Chlamydia notification rates, however, rose 2.4-fold between 1995 and 2000 (16.1/10(5) to 54.2/10(5)). In the same period there was a 218% increase the reported incidence of genital herpes. STIs are more common in the eastern industrial regions. In the period 1994-7 there was a dramatic 179-fold increase in the prevalence of HIV/AIDS which has plateaued in subsequent years. By January 2001 a total of 36,600 cases of HIV infection (including 2040 people with AIDS) have been reported. The proportion of HIV acquired through injecting drug use is falling (72.7% in 1997 to 54.2% in 2000) in relation to that acquired through sexual contact. CONCLUSIONS: STIs and HIV are a common cause of morbidity in Ukraine.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12238659&dopt=Abstract

J Virol. 2002 Oct;76(20):10270-81.
Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.

Chaudhuri M, Parris DS.

Department of Molecular Virology, Immunology and Medical Genetics, Comprehensive Cancer Center, Ohio State University, 333W. Tenth Avenue, Columbus, OH 43210, USA.

The DNA polymerase holoenzyme of herpes simplex virus type 1 (HSV-1) is a stable heterodimer consisting of a catalytic subunit (Pol) and a processivity factor (UL42). HSV-1 UL42 differs from most DNA polymerase processivity factors in possessing an inherent ability to bind to double-stranded DNA. It has been proposed that UL42 increases the processivity of Pol by directly tethering it to the primer and template (P/T). To test this hypothesis, we took advantage of the different sensitivities of Pol and Pol/UL42 activities to ionic strength. Although the activity of Pol is inhibited by salt concentrations in excess of 50 mM KCl, the activity of the holoenzyme is relatively refractory to changes in ionic strength from 50 to 125 mM KCl. We used nitrocellulose filter-binding assays and real-time biosensor technology to measure binding affinities and dissociation rate constants of the individual subunits and holoenzyme for a short model P/T as a function of the ionic strength of the buffer. We found that as observed for activity, the binding affinity and dissociation rate constant of the Pol/UL42 holoenzyme for P/T were not altered substantially in high- versus low-ionic-strength buffer. In 50 mM KCl, the apparent affinity with which UL42 bound the P/T did not differ by more than twofold compared to that observed for Pol or Pol/UL42 in the same low-ionic-strength buffer. However, increasing the ionic strength dramatically decreased the affinity of UL42 for P/T, such that it was reduced more than 3 orders of magnitude from that of Pol/UL42 in 125 mM KCl. Real-time binding kinetics revealed that much of the reduced affinity could be attributable to an extremely rapid dissociation of UL42 from the P/T in high-ionic-strength buffer. The resistance of the activity, binding affinity, and stability of the holoenzyme for the model P/T to increases in ionic strength, despite the low apparent affinity and poor stability with which UL42 binds the model P/T in high concentrations of salt, suggests that UL42 does not simply tether the Pol to DNA. Instead, it is likely that conformational alterations induced by interaction of UL42 with Pol allow for high-affinity and high-stability binding of the holoenzyme to the P/T even under high-ionic-strength conditions.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12239303&dopt=Abstract

J Virol. 2002 Oct;76(20):10320-31.
Functional dissection of latency-associated nuclear antigen 1 of Kaposi's sarcoma-associated herpesvirus involved in latent DNA replication and transcription of terminal repeats of the viral genome.

Lim C, Sohn H, Lee D, Gwack Y, Choe J.

Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.

Latency-associated nuclear antigen 1 (LANA1) of Kaposi's sarcoma-associated herpesvirus (KSHV) is implicated in the maintenance of the viral genome during latent infection. LANA1 colocalizes with KSHV episomes on the host chromosome and mediates their maintenance by attaching these viral structures to host chromosomes. Data from long-term selection of drug resistance in cells conferred by plasmids containing the terminal repeat (TR) sequence of KSHV revealed that KSHV TRs and LANA1 act as cis and trans elements of viral latent replication, respectively. In this study, we further characterized the cis- and trans-acting elements of KSHV latent replication by using a transient replication assay with a methylation-sensitive restriction enzyme, DpnI. Transient reporter and replication assays disclosed that the orientation and basal transcriptional activity of TR constructs did not significantly affect the efficiency of replication. However, at least two TR units were necessary for efficient replication. The N-terminal 90 amino acids comprising the chromosome-binding domain of LANA1 were required for the mediation of LANA1 C-terminal DNA-binding and dimerization domains to support the transient replication of KSHV TRs. LANA1 interacted with components of the origin recognition complexes (ORCs), similar to Epstein-Barr virus nuclear antigen 1. Our data suggest that LANA1 recruits ORCs to KSHV TRs for latent replication of the viral genome.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12239308&dopt=Abstract

J Virol. 2002 Oct;76(20):10338-45.
Phenotypic and functional alterations of dendritic cells induced by human herpesvirus 6 infection.

Kakimoto M, Hasegawa A, Fujita S, Yasukawa M.

First Department of Internal Medicine, Ehime University School of Medicine, Shigenobu, Ehime 791-0295, Japan.

Human herpesvirus 6 (HHV-6) has a tropism for T lymphocytes and monocytes/macrophages, suggesting that HHV-6 infection affects the immunosurveillance system. In the present study, we investigated the HHV-6-induced phenotypic and functional alterations of dendritic cells (DCs), which are professional antigen-presenting cells. HHV-6 infection of monocyte-derived immature DCs appeared to induce the up-regulation of CD80, CD83, CD86, and HLA class I and class II molecules, suggesting that HHV-6 infection induces the maturation of DCs. In addition, the antigen capture capacity of DCs was found to decrease following infection with HHV-6. In contrast to up-regulation of mature-DC-associated surface molecules on HHV-6-infected DCs, their capacity for presentation of alloantigens and exogenous virus antigens to T lymphocytes decreased significantly from that of uninfected DCs. In contrast, there appeared to be no reduction in the capacity for presentation of an HLA class II-binding peptide to the peptide-specific CD4(+) T lymphocytes. These data indicate that HHV-6 infection induces phenotypic alterations and impairs the antigen presentation capacity of DCs. The present data also suggest that the dysfunction of HHV-6-infected DCs is attributable mainly to impairment of the antigen capture and intracellular antigen-processing pathways.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12239310&dopt=Abstract

J Virol. 2002 Oct;76(20):10365-73.
Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains.

Hutchinson I, Whiteley A, Browne H, Elliott G.

Virus Assembly Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK.

The subcellular localization of herpes simplex virus tegument proteins during infection is varied and complex. By using viruses expressing tegument proteins tagged with fluorescent proteins, we previously demonstrated that the major tegument protein VP22 exhibits a cytoplasmic localization, whereas the major tegument protein VP13/14 localizes to nuclear replication compartments and punctate domains. Here, we demonstrate the presence of a second minor population of VP22 in nuclear dots similar in appearance to those formed by VP13/14. We have constructed the first-described doubly fluorescence-tagged virus expressing VP22 and VP13/14 as fusion proteins with cyan fluorescent protein and yellow fluorescent protein, respectively. Visualization of both proteins within the same live infected cells has indicated that these two tegument proteins localize to the same nuclear dots but that VP22 appears there earlier than VP13/14. Further studies have shown that these tegument-specific dots are detectable as phase-dense bodies as early as 2 h after infection and that they are different from the previously described nuclear domains that contain capsid proteins. They are also different from the ICP0 domains formed at cellular nuclear domain 10 sites early in infection but, in almost all cases, are located in juxtaposition to these ICP0 domains. Hence, these tegument proteins join a growing number of proteins that are targeted to discrete nuclear domains in the herpesvirus-infected cell nucleus.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12239313&dopt=Abstract

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