A Phase II Proof of Concept Multicenter, Randomized, Double-Blind Study to Assess the Safety and Efficacy of Phage Therapy in Patients with Hip or Knee Prosthetic Joint Infection Due to Staphylococcus Aureus Treated by DAIR

Total joint replacements are effective for chronic pain but can lead to Prosthetic Joint Infections (PJI), primarily caused by Staphylococcus aureus and resistant to antibiotics. Standard treatment involves DAIR surgery and antibiotics, but there's a need for better solutions due to rising infections and antibiotic resistance. Bacteriophage therapy, which targets specific bacteria, shows promise. Phaxiam Therapeutics is studying the safety and efficacy of phage therapy in treating Staphylococcus aureus infections in hip or knee PJI patients undergoing DAIR.

开始日期2025-01-01

申办/合作机构

PHAXIAM Therapeutics SA

NCT02357966 / Completed临床1/2期

A Phase I-II Study of the Safety and Efficacy of a True Human Antibody, 514G3, in Subjects Hospitalized With Bacteremia Due to Staphylococcus Aureus

This study will evaluate the maximum safe dose of the true human monoclonal antibody, 514G3, in the treatment of patients with Staphylococcus Aureus bacteremia. Preliminary evidence of efficacy will be evaluated as well. Patients will receive 514G3 plus antibiotics or placebo plus antibiotics in approximately a 3 to 1 ratio.

开始日期2015-05-01

申办/合作机构

XBiotech, Inc.

NCT00113191 / CompletedN/A

A Phase III, Randomized, Double-blind, Multi-center Clinical Trial Comparing the Safety and Efficacy of Veronate® Versus Placebo for the Prevention of Nosocomial Staphylococcal Sepsis in Premature Infants (Birth Weight 500 - 1250 g)

The purpose of this study is to show whether Veronate, a donor-selected staphylococcal human immune globulin intravenous (IGIV), can prevent an infection in the blood caused by staphylococcal bacteria in premature babies weighing between 500 and 1250 grams at birth.
Babies are enrolled between Day of Life 3 and 5. Babies are randomized to either Veronate or placebo (50-50 chance of either). Babies can receive up to 4 doses of the study drug on Study Days 1, 3, 8 and 15 and are followed until Study Day 70 or discharge from the hospital.

开始日期2004-05-01

申办/合作机构

Bristol Myers Squibb Co.

100 项与 SA ClfA 相关的临床结果

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100 项与 SA ClfA 相关的转化医学

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0 项与 SA ClfA 相关的专利（医药）

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项与 SA ClfA 相关的文献（医药）

2024-04-01·Heliyon

Anti-Staphylococcus aureus potential of compounds from Ganoderma sp.: A comprehensive molecular docking and simulation approaches

Article

作者: Tran, Linh Thuoc ; Nguyen, Tan Khanh ; Truong, Phu Chi Hieu ; Nguyen, Trang Thi Thu ; Nguyen, Trinh Thi Tuyet ; Tran, Linh Thuy Thi ; Tran, Manh Hung ; Nguyen, Hoang Duc ; Pham, Phu Tran Vinh ; Pham, Hong Khuyen Thi

In this study, a series of secondary metabolites from Ganoderma sp. were screened against Staphylococcus aureus protein targets, including as phosphotransacetylase, clumping factor A, and dihydrofolate reductase, using molecular docking simulations. The chemicals that showed the strongest binding energy with the targeted proteins were ganodermanontriol, lucidumol B, ganoderic acid J, ergosterol, ergosterol peroxide, 7-oxoganoderic acid Z, ganoderic acid AM1, ganosinoside A, ganoderic acid D, and 24R-ergosta-7,2E-diene-3β,5α,6β-triol. Interestingly, ganosinoside A showed the greatest affinity for the protein clumping factor A, a result validated by molecular dynamic simulation. Additionally, three natural Ganoderma sp. Strains as Ganoderma lingzhi VNKKK1903, Ganoderma lingzhi VNKK1905A2, and Amauroderma subresinosum VNKKK1904 were collected from Kon Ka Kinh National Park in central land of Vietnam and evaluated for their antibacterial activity against Staphylococcus aureus using an agar well diffusion technique. These results suggest that the fungal extracts and secondary metabolites may serve as valuable sources of antibiotics against Staphylococcus aureus. These findings provided an important scientific groundwork for further exploration of the antibacterial mechanisms of compounds derived from Ganoderma sp. in future research.

2024-02-01·International Journal of Biological Macromolecules

Development of nanobodies specific to clumping factors A of Staphylococcus aureus by yeast surface display

Article

作者: Hu, Yang ; Ren, Xinyi ; Xing, Banbin ; Ming, Ke ; Yi, Li ; Chen, Huan ; Wang, Longhao ; Li, Shiqi ; Lu, Mengqing ; Wei, Zigong ; Mei, Meng ; Wu, Yuqi

The Staphylococcus aureus clumping factor A (ClfA) is a fibrinogen (Fg) binding protein that plays an important role in the clumping of S. aureus in blood plasma. The current anti-infective approaches targeting ClfA are mainly based on monoclonal antibodies but showed less impressive efficacy for clinical applications. Nanobodies offer advantages in enhanced tissue penetration and a propensity to bind small epitopes. However, there is no report on generating specific nanobodies for ClfA. Here, we constructed a synthetic nanobody library based on yeast surface display to isolate nanobodies against the Fg binding domain ClfA₂₂₁_-₅₅₀. We firstly obtained a primary nanobody directed to ClfA₂₂₁_-₅₅₀, and then employed error-prone mutagenesis to enhance its binding affinity. Finally, 18 variants were isolated with high affinities (EC50, 1.1 ± 0.1 nM to 4.8 ± 0.3 nM), in which CNb1 presented the highest inhibition efficiency in the adhesion of S. aureus to fibrinogen. Moreover, structural simulation analysis indicated that the epitope for CNb1 partially overlapped with the binding sites for fibrinogen, thus inhibiting ClfA binding to Fg. Overall, these results indicated that the specific nanobodies generated here could prevent the adhesion of S. aureus to fibrinogen, suggesting their potential capacities in the control of S. aureus infections.

2017-12-01·Infection and Immunity2区 · 医学

The Staphylococcus aureus Cell Wall-Anchored Protein Clumping Factor A Is an Important T Cell Antigen

2区 · 医学

Article

作者: Lalor, Stephen J. ; Lacey, Keenan A. ; Geoghegan, Joan A. ; McCormack, Niamh ; McLoughlin, Rachel M. ; Leech, John M.

ABSTRACTStaphylococcus aureus has become increasingly resistant to antibiotics, and vaccines offer a potential solution to this epidemic of antimicrobial resistance. Targeting of specific T cell subsets is now considered crucial for next-generation anti- S. aureus vaccines; however, there is a paucity of information regarding T cell antigens of S. aureus . This study highlights the importance of cell wall-anchored proteins as human CD4 + T cell activators capable of driving antigen-specific Th1 and Th17 cell activation. Clumping factor A (ClfA), which contains N1, N2, and N3 binding domains, was found to be a potent human T cell activator. We further investigated which subdomains of ClfA were involved in T cell activation and found that the full-length ClfA N123 and N23 were potent Th1 and Th17 activators. Interestingly, the N1 subdomain was capable of exclusively activating Th1 cells. Furthermore, when these subdomains were used in a model vaccine, N23 and N1 offered Th1- and Th17-mediated systemic protection in mice upon intraperitoneal challenge. Overall, however, full-length ClfA N123 is required for maximal protection both locally and systemically.