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Identification
- Summary
Crotalus atrox antivenin is a mixture of antibodies used to treat venomous snake bites from Crotalus atrox (Western Diamondback rattlesnake).
- Brand Names
- Crofab
- Generic Name
- Crotalus atrox antivenin
- DrugBank Accession Number
- DB13892
- Background
Each year it is estimated there are 45,000 snakebites in the US and 300,000 to 400,000 bites worldwide. About 8000 of these snakebites involve venomous snake species. The majority of people bitten are males and about 50% occur in the age group of 18 to 28 10.
Crotalus atrox antivenin is derived and purified immunoglobulin fragments obtained from other domestic animals such as sheep previously immunized with Crotalus atrox (Western Diamondback rattlesnake). Bites from this snake are the most common in the state of Texas, USA 3.
The final purified antivenin product is produced by mixing other different monospecific snake antivenins and isolating the antivenin of interest through fractionation and chromatography techniques. It is intravenously (IV) administered to prevent/limit systemic toxicity Label.
- Type
- Biotech
- Groups
- Approved, Experimental
- Biologic Classification
- Protein Based Therapies
Other protein based therapies - Protein Chemical Formula
- Not Available
- Protein Average Weight
- Not Available
- Sequences
- Not Available
- Synonyms
- Crotalus atrox immune fab antivenin (ovine)
Pharmacology
- Indication
CROFAB is indicated for the management of adult and pediatric patients with North American crotalid envenomation. The term crotalid is used to describe the Crotalinae subfamily (formerly known as Crotalidae) of venomous snakes which includes rattlesnakes, copperheads and cottonmouths/water moccasins Label.
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Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Reversal of Venom poisoning caused by crotalus atrox •••••••••••• - Contraindications & Blackbox Warnings
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Crotalus atrox venom contains agents that render human fibrinogen and plasma incoagulable by thrombin 4. CROFAB antivenom reverses these effects Label.
This facilitates re-distribution of venom toxins away from target tissues and elimination from the body 8.
It is a mixture of 4 different monospecific antivenoms derived from serum of healthy sheep immunized with one of the following North American snake venoms: C. atrox (Western diamondback rattlesnake), C. adamanteus (Eastern diamondback rattlesnake), C. scutulatus (Mojave rattlesnake), or A. piscivorus (cottonmouth or water moccasin) 8.
- Mechanism of action
CROFAB consists of venom-specific Fab fragments of immunoglobulin G (IgG) that work by binding to and neutralizing venom toxins, facilitating their redistribution away from target tissues and their elimination from the body 6.
CROFAB contains only the Fab fragments from ovine-derived immunoglobulins. The enzyme papain is used to cleave the IgG antibody, creating 2 separate Fab fragments and 1 Fc fragment. After the cleavage step, another protein binds to the Fc fragments, which are not essential for binding snake venom, allowing the pure Fab fragments to be recovered.The Fab fragments of an immunoglobulin contain the variable regions that recognize and bind to specific antigens 6.
- Absorption
Not Available
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
12-23 hours 10
- Clearance
Not Available
- Adverse Effects
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Most common adverse reactions (incidence ≥5% of subjects) were urticaria, rash nausea, pruritus and back pain Label.
Severe hypersensitivity reactions may occur with the use of CROFAB. In case of acute hypersensitivity reactions, including anaphylaxis and anaphylactoid reactions, discontinue infusion and institute appropriate emergency treatment Label.
CROFAB contains purified immunoglobulin fragments from the blood of sheep that have been immunized with snake venoms. Injection of heterologous animal proteins can lead to severe acute and delayed hypersensitivity reactions (late serum reaction or serum sickness) and a possible febrile response to immune complexes formed by animal antibodies and neutralized venom components.
Papain enzyme is used to cleave antibodies into fragments during the processing of CROFAB, and negligible amounts of papain or inactivated papain residues may be present. Patients allergic to papain, chymopapain, other papaya extracts, or the pineapple enzyme bromelain may also have an allergic reaction to CROFAB. Certain dust mite allergens and some latex allergens share antigenic structures with papain and patients with these allergies may be allergic to papain Label.
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.Not Available
- Food Interactions
- No interactions found.
Products
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Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image CroFab Crotalus atrox antivenin (1 g/1) + Agkistrodon piscivorus antivenin (1 g/1) + Crotalus adamanteus antivenin (1 g/1) + Crotalus scutulatus antivenin (1 g/1) Injection, powder, lyophilized, for solution Intravenous BTG International Inc. 2000-02-10 Not applicable US 
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- Not Available
- Kingdom
- Organic Compounds
- Super Class
- Organic Acids
- Class
- Carboxylic Acids and Derivatives
- Sub Class
- Amino Acids, Peptides, and Analogues
- Direct Parent
- Peptides
- Alternative Parents
- Not Available
- Substituents
- Not Available
- Molecular Framework
- Not Available
- External Descriptors
- Not Available
- Affected organisms
- Humans
Chemical Identifiers
- UNII
- RBR61YAJ4V
- CAS number
- Not Available
References
- General References
- de Rezende NA, Torres FM, Dias MB, Campolina D, Chavez-Olortegui C, Amaral CF: South American rattlesnake bite (Crotalus durissus SP) without envenoming: insights on diagnosis and treatment. Toxicon. 1998 Dec;36(12):2029-32. [Article]
- Seifert SA, Boyer LV, Dart RC, Porter RS, Sjostrom L: Relationship of venom effects to venom antigen and antivenom serum concentrations in a patient with Crotalus atrox envenomation treated with a Fab antivenom. Ann Emerg Med. 1997 Jul;30(1):49-53. [Article]
- Rosen PB, Leiva JI, Ross CP: Delayed antivenom treatment for a patient after envenomation by Crotalus atrox. Ann Emerg Med. 2000 Jan;35(1):86-8. [Article]
- Pandya BV, Budzynski AZ: Anticoagulant proteases from western diamondback rattlesnake (Crotalus atrox) venom. Biochemistry. 1984 Jan 31;23(3):460-70. [Article]
- Delayed antivenom treatment for a patient after envenomation by Crotalus atrox [Link]
- CROFAB.COM [Link]
- Epocrates online, Crofab [Link]
- Drugs.com, Crofab [Link]
- Crotalus atrox PhospholipaseAz [File]
- Crotalidae Polyvalent Immune Fab (Ovine) [File]
- External Links
- FDA label
- Download (407 KB)
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample data4 Completed Treatment Snake Bite 1 somestatus stop reason just information to hide 4 Terminated Treatment Snake Envenomation 1 somestatus stop reason just information to hide 3 Completed Treatment Snake Bite 1 somestatus stop reason just information to hide 2 Completed Treatment Coagulation Disorder / Snake Bite 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Injection, powder, lyophilized, for solution Intravenous - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Not Available
- Experimental Properties
- Not Available
Enzymes
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids (PubMed:12021277, PubMed:9188469). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids with preference for phosphatidylcholines and phosphatidylglycerols over phosphatidylethanolamines. Preferentially releases sn-2 omega-6 and omega-3 polyunsaturated fatty acyl (PUFA) chains over saturated fatty acyls (PubMed:12021277, PubMed:12359733). Contributes to phospholipid remodeling of very low-density lipoprotein (VLDL), low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles (PubMed:12021277). Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells (PubMed:12021277). Efficiently hydrolyzes and inactivates platelet activating factor (PAF), a potent lipid mediator present in oxidized LDL (PubMed:16962371). May act in an autocrine and paracrine manner. Secreted by lung epithelium, targets membrane phospholipids of infiltrating eosinophils, releasing arachidonate and boosting eicosanoid and cysteinyl leukotriene synthesis involved in airway inflammatory response (By similarity). Secreted by gut epithelium, hydrolyzes dietary and biliary phosphatidylcholines in the gastrointestinal lumen (By similarity). Plays a stem cell regulator role in colon epithelium. Within intracellular compartment, mediates Paneth-like cell differentiation and its stem cell supporting functions by inhibiting the Wnt signaling pathway in intestinal stem cell (ISC). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ISCs and tissue regeneration (By similarity). May participate in hair follicle morphogenesis by regulating phosphatidylethanolamines metabolism at the outermost epithelial layer and facilitating melanin synthesis (By similarity). By releasing lysophosphatidylcholines (LPCs) at sperm acrosome, controls sperm cell capacitation, acrosome reaction and overall fertility (By similarity). May promote neurite outgrowth in neuron fibers involved in nociception (By similarity). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria (PubMed:12359733). Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (PubMed:11694541). In pulmonary epithelium, may contribute to host defense response against adenoviral infection. Prevents adenovirus entry into host cells by hydrolyzing host cell plasma membrane, releasing C16:0 LPCs that inhibit virus-mediated membrane fusion and viral infection. Likely prevents adenoviral entry into the endosomes of host cells (PubMed:16146426). May play a role in maturation and activation of innate immune cells including macrophages, group 2 innate lymphoid cells and mast cells (By similarity)
- Specific Function
- 1-alkyl-2-acetylglycerophosphocholine esterase activity
- Gene Name
- PLA2G10
- Uniprot ID
- O15496
- Uniprot Name
- Group 10 secretory phospholipase A2
- Molecular Weight
- 18153.04 Da
References
- Walton RM, Brown DE, Hamar DW, Meador VP, Horn JW, Thrall MA: Mechanisms of echinocytosis induced by Crotalus atrox venom. Vet Pathol. 1997 Sep;34(5):442-9. doi: 10.1177/030098589703400508. [Article]
- Sanny CG: In vitro evaluation of total venom-antivenin immune complex formation and binding parameters relevant to antivenin protection against venom toxicity and lethality based on size-exclusion high-performance liquid chromatography. Toxicon. 2011 May;57(6):871-81. doi: 10.1016/j.toxicon.2011.03.003. Epub 2011 Mar 15. [Article]
- Perumal Samy R, Gopalakrishnakone P, Chow VT: Therapeutic application of natural inhibitors against snake venom phospholipase A(2). Bioinformation. 2012;8(1):48-57. doi: 10.6026/97320630008048. Epub 2012 Jan 6. [Article]
Drug created at September 08, 2017 20:22 / Updated at June 19, 2021 00:27