Vaborbactam

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Vaborbactam.svg

Vaborbactam is a beta-lactamase inhibitor used in combination with the antibiotic meropenem to treat certain serious bacterial infections. It is particularly effective against carbapenem-resistant Enterobacteriaceae (CRE), which are a significant cause of hospital-acquired infections.

Mechanism of Action[edit | edit source]

Vaborbactam works by inhibiting the activity of beta-lactamase enzymes produced by bacteria. These enzymes typically break down beta-lactam antibiotics, rendering them ineffective. By inhibiting these enzymes, vaborbactam allows meropenem to retain its antibacterial activity against resistant strains.

Clinical Use[edit | edit source]

Vaborbactam is used in combination with meropenem for the treatment of complicated urinary tract infections (cUTIs), including pyelonephritis, and for the treatment of complicated intra-abdominal infections (cIAIs). It is also used for the treatment of hospital-acquired pneumonia and ventilator-associated pneumonia.

Pharmacokinetics[edit | edit source]

Vaborbactam is administered intravenously and has a half-life that allows for dosing every 8 hours when combined with meropenem. It is primarily excreted unchanged in the urine.

Side Effects[edit | edit source]

Common side effects of vaborbactam include headache, nausea, diarrhea, and infusion site reactions. Serious side effects may include allergic reactions and seizures.

Approval and Availability[edit | edit source]

Vaborbactam was approved by the Food and Drug Administration (FDA) in 2017 for use in combination with meropenem. It is marketed under the brand name Vabomere.

See Also[edit | edit source]

References[edit | edit source]


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Engineered Monoclonal Antibodies[edit source]

Diagram of engineered monoclonal antibodies

Engineered monoclonal antibodies are a class of biological therapies that are designed to target specific antigens on the surface of cells. These antibodies are produced using recombinant DNA technologies and are used in the treatment of various diseases, including cancer, autoimmune disorders, and infectious diseases.

Structure and Function[edit source]

Monoclonal antibodies are composed of two identical heavy chains and two identical light chains, forming a Y-shaped molecule. The tips of the "Y" contain the antigen-binding sites, which are highly specific to the target antigen. This specificity allows monoclonal antibodies to bind to their target with high affinity, blocking or modulating the function of the antigen.

Types of Engineered Monoclonal Antibodies[edit source]

There are several types of engineered monoclonal antibodies, each designed for specific therapeutic purposes:

  • Chimeric antibodies: These antibodies are composed of murine (mouse) variable regions and human constant regions. They are less immunogenic than fully murine antibodies.
  • Humanized antibodies: These antibodies are mostly human, with only the antigen-binding sites derived from murine sources. This reduces the risk of immune reactions.
  • Fully human antibodies: These are entirely human in origin, produced using transgenic mice or phage display technologies.
  • Bispecific antibodies: These antibodies are engineered to bind two different antigens simultaneously, offering unique therapeutic mechanisms.

Applications in Medicine[edit source]

Engineered monoclonal antibodies have revolutionized the treatment of many diseases:

  • Cancer therapy: Monoclonal antibodies can target specific tumor antigens, leading to direct tumor cell killing or recruitment of immune cells to attack the tumor.
  • Autoimmune diseases: By targeting specific components of the immune system, monoclonal antibodies can reduce inflammation and tissue damage in diseases such as rheumatoid arthritis and multiple sclerosis.
  • Infectious diseases: Monoclonal antibodies can neutralize pathogens or their toxins, providing passive immunity or enhancing the host's immune response.

Production[edit source]

The production of engineered monoclonal antibodies involves several steps:

1. Antigen identification: The target antigen is identified and characterized. 2. Hybridoma technology: B cells from immunized animals are fused with myeloma cells to create hybridomas that produce the desired antibody. 3. Recombinant DNA technology: Genes encoding the antibody are cloned and expressed in suitable host cells, such as Chinese hamster ovary cells. 4. Purification and formulation: The antibodies are purified and formulated for clinical use.

Challenges and Future Directions[edit source]

While engineered monoclonal antibodies have shown great promise, there are challenges such as high production costs, potential for immune reactions, and the development of resistance. Ongoing research aims to improve antibody design, reduce immunogenicity, and enhance therapeutic efficacy.

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