Monday Parallel Session 18, October 30, 2006

HCV: Pre-Clinical and Early Development

 

127. Phase I single-dose study of bavituximab, a chimeric anti-phosphatidylserine monoclonal antibody, in subjects with chronic hepatitis C. 

E. W. Godofsky; J. S. Shan.

Background:

Bavituximab is a novel monoclonal antibody that specifically targets phosphatidylserine (PS) on the outer surface of the plasma membrane of virally infected cells and enveloped viruses. Once bound, it is believed to direct the host’s immune system to clear virally infected cells and viruses. Its antiviral activity has been previously demonstrated in animal models of murine cytomegalovirus and pichinde virus.

 

Aim:

To determine the safety, tolerability and pharmacokinetics of a single intravenous (IV) infusion of bavituximab in a phase I, open-label, dose-escalation study in subjects with chronic HCV infection who failed to respond to or relapsed after pegylated interferon plus ribavirin combination therapy.

 

Methods:

Sequential cohorts of 6 subjects were given a single 90 min IV infusion of bavituximab at 0.1, 0.3, 1, 3 or 6 mg/kg and were followed for 12 weeks. Vital signs, physical exams, safety laboratory parameters, serum bavituximab levels were monitored and serum HCV RNA levels were measured by NGI SuperQuant.

 

Results:

The infusion was safe and well tolerated by all subjects. All adverse events were mild or moderate in severity, except for 1 report of severe headache at 1 mg/kg and 1 of severe vertigo at 3mg/kg, both unrelated to study drug. The majority of AEs were considered not related to study drug, with the most common being injection site bruises, nausea, rhinitis, and headache. There were no laboratory AEs except for expected subclinical transient prolongation of aPTT for the 3 and 6 mg/kg dose groups on day 1 postdose. After IV infusion, bavituximab reaches Cmax at 1h postdose with a mean elimination half-life of ~31h. There was a trend towards a bimodal decrease in mean serum HCV RNA levels. The first decrease was seen within 24 hours postdose and the second began around day 4 and appeared sustained up to several weeks in some subjects. Serum cytokine analyses are ongoing.

 

Conclusions:

Single IV doses of bavituximab up to 6 mg/kg were safe and well tolerated. It has a predictable pharmacokinetic profile. The transient reductions in serum viral load were consistent with the proposed mechanism of immune stimulation. Unlike conventional therapy, bavituximab is a unique therapeutic that targets viruses and virally infected cells by channeling host’s defense against them. Since it does not target viral proteins, bavituximab is unlikely to elicit traditional viral resistance.

 


128. Discovery, Characterization and Anti-HCV Activity of a Novel NS5B Inhibitor. 

R. Wagner; D. Larson; T. Bosse; W. Kati; H. Mo; G. Koev; S. Masse; W. Jiang; Y. Liu; D. Montgomery; T. Middleton; V. S. Stoll; K. D. Stewart; D. Beno; R. Lanford; W. Kohlbrenner; D. Kempf; A. Molla.

Background:

The identification of small-molecule drugs to treat HCV infection is an area of intense research. Combinations of such agents have the potential to avoid resistance emergence and yield higher SVR with fewer side effects. We report the discovery of a new potent HCV polymerase inhibitor, A-837093, with excellent pharmacokinetics (PK), that shows “viral clearance” in the replicon assay in combination with another small molecule inhibitor and has demonstrated efficacy in the chimpanzee.

 

Methods:

In vitro activity was measured in subgenomic HCV genotype 1a and 1b replicons. Resistant replicon colonies were selected by treating replicon cells with A-837093 at a concentration 10x above its EC50. Rats, monkeys and dogs were dosed orally at 5 mpk and plasma levels of A-837093 were determined by HPLCMS. HCV drug-naive genotype 1a- and 1b-infected chimpanzees were dosed orally with a suspension of A-837093 for 14 days at 30 mpk BID. Blood samples were periodically withdrawn to determine viral load, viral sequence, plasma trough drug levels and clinical chemistry parameters.

 

Results:

A-837093, a subnanomolar enzyme inhibitor, inhibits HCV genotype 1 with EC50s of 3-11 nM. In the presence of 40% human serum, EC50s are attenuated up to 17-fold. A-837093-treated replicon cells produced resistant colonies that contained 1-3 mutations within the NS5B gene, resulting in potency losses >800- fold relative to the wild-type (WT) replicon. However, the combination of A-837093 and the HCV protease inhibitor BILN-2061 produced a synergistic antiviral effect and prevented development of resistance, “curing” the replicon cells. Replication efficiency of mutant replicons was impaired compared with the WT replicon. Oral bioavailability of A-837093 was 62% in rat, 100% in dog and 19% in monkey, partitioning into liver tissue (20:1 rat, 200:1 monkey) relative to plasma. Dosing in 1a- and 1b-infected chimpanzees after 2 days at 30 mpk, resulted in a 1.4 log10 and 2.5 log10 drop in HCV RNA, respectively. By day 5, plasma HCV RNA in the 1b-infected animal rebounded to within 0.6 log10 copies/mL of baseline, while the 1a-infected chimpanzee experienced a sustained viral load reduction throughout the treatment period.

 

Conclusion:

We have demonstrated that A-837093 is an efficacious inhibitor of HCV infection in the chimpanzee model. While successful therapy with any single agent is unlikely, in vitro combination studies suggest that A-837093 may be useful in combination with other small-molecule HCV inhibitors to effectively treat HCV infection.

 


129. Telaprevir (TVR, VX-950) resistance variants A156T/V exhibit reduced cleavage of innate immunity signaling proteins, TRIF and IPS-1. 

G. Kalkeri; B. Rao; D. Brennan; A. Kwong.

Introduction/Purpose:

More than 80% of Hepatitis C virus (HCV) infections result chronic hepatitis C. However, the factors responsible for viral persistence/immune evasion are not clearly understood. HCV NS3/4A protease is implicated in viral evasion of TLR3 or Rig- I mediated innate immunity by cleaving the TRIF and IFN-b promoter stimulator 1 (IPS-1) protein adaptors respectively. Cleavage of IPS-1 is observed in HCV infections both in vitro and in vivo1. Telaprevir (TVR, VX-950) is a highly selective inhibitor of the HCV NS3/4A protease that has demonstrated strong antiviral activity in patients with genotype 1 HCV when dosed alone, or with peginterferon (PEG-IFN) but has demonstrated the existence of NS3 variants with reduced sensitivity to telaprevir. The purpose of this study was to compare the cleavage of viral (5A/B) and innate immunity (TRIF and IPS-1) substrates by HCV proteases from different genotypes (1b, 2a & 3a), to demonstrate the inhibition of this cleavage by telaprevir, and to test the ability of telaprevir resistance mutants to cleave these substrates.

 

Methods:

In vitro cleavage reactions of 35S-labeled HCV (5A/B) and TRIF & IPS-1 substrates were performed and quantified. Computational modeling analysis was performed using Quanta Molecular Mechanics program.

Results: NS3/4A protease from HCV genotypes 1, 2 and 3 were able to cleave TRIF and IPS-1. Telaprevir, which inhibits cleavage of the natural HCV substrate (5A/B), was also able to inhibit the genotype 1 HCV protease-mediated cleavage of TRIF in a similar manner. This supports a hypothesis wherein telaprevir might play a dual role in the treatment of HCV infections by acting as a direct antiviral agent as well as restoring innate immunity.

 

A156V/T variants with reduced sensitivity to telaprevir and impaired viral fitness compared to wild type virus have been reported in vitro2 and in vivo3. These in vitro telaprevir-resistant mutants were found to have significantly reduced ability to cleave HCV 5A/B consistent with their poor replicative fitness. Cleavage of TRIF & IPS-1 substrates by these mutants was also impaired. Computational modeling suggests that steric hindrance might decrease binding of TRIF to the A156T/V mutant protease, resulting in inefficient cleavage.

 

Conclusion:

The A156V/T variants exhibit impaired cleavage of TRIF and IPS-1, suggesting that the emergence of these telaprevir resistance mutants may not compromise the potential restoration of innate immunity by telaprevir.

1) Loo et al (2006) PNAS, 103:6001-6006

2) Lin et al (2005) JBC 280:36784-36791

3) Sarrazin, et al (2005) AASLD, Abst LB06.