Cobra venom factor (CVF) is a protein found in cobra venom that functions as a complement-activating protein [1] [2] [3] [4] [5] [6]. It is structurally and functionally similar to complement component C3b [3] [5]. CVF has been used for decomplementation of serum to investigate the role of complement in various disease model systems [4]. In terms of its main functions, CVF is known to activate the complement system, leading to complement depletion [1] [4]. This protein plays a role in complement activation and complement depletion, resembling the function of C3b [3] [5]. Additionally, CVF has been shown to boost arteriogenesis in mice [7]. Furthermore, CVF is a major functional category represented in the proteome of cervical-vaginal fluid (CVF), emphasizing its significance in the immune response [8] [9].
References:
[1] C. Vogel, D. Fritzinger, W. Gorsuch, & G. Stahl, "Complement depletion with humanised cobra venom factor: efficacy in preclinical models of vascular diseases", Thrombosis and Haemostasis, vol. 113, no. 03, p. 548-552, 2015. https://doi.org/10.1160/th14-04-0300
[2] C. Vogel and D. Fritzinger, "Humanized cobra venom factor: experimental therapeutics for targeted complement activation and complement depletion", Current Pharmaceutical Design, vol. 13, no. 28, p. 2916-2926, 2007. https://doi.org/10.2174/138161207782023748
[3] K. Wong, K. Tan, N. Tan, & C. Tan, "A neurotoxic snake venom without phospholipase a2: proteomics and cross-neutralization of the venom from senegalese cobra, naja senegalensis (subgenus: uraeus)", Toxins, vol. 13, no. 1, p. 60, 2021. https://doi.org/10.3390/toxins13010060
[4] W. Gorsuch, B. Guikema, D. Fritzinger, C. Vogel, & G. Stahl, "Humanized cobra venom factor decreases myocardial ischemia–reperfusion injury", Molecular Immunology, vol. 47, no. 2-3, p. 506-510, 2009. https://doi.org/10.1016/j.molimm.2009.08.017
[5] A. Manuwar, B. Dreyer, A. Böhmert, A. Ullah, Z. Mughal, A. Akremet al., "Proteomic investigations of two pakistani naja snake venoms species unravel the venom complexity, posttranslational modifications, and presence of extracellular vesicles", Toxins, vol. 12, no. 11, p. 669, 2020. https://doi.org/10.3390/toxins12110669
[6] S. Sharma, T. Jabeen, R. Singh, R. Bredhorst, C. Vogel, & C. Betzel, "Structural studies on the cobra venom factor: isolation, purification, crystallization and preliminary crystallographic analysis", Acta Crystallographica Section D Biological Crystallography, vol. 57, no. 4, p. 596-598, 2001. https://doi.org/10.1107/s0907444901001342
[7] P. Götz, S. Azubuike-Osu, A. Braumandl, C. Arnholdt, M. Kübler, L. Richteret al., "Cobra venom factor boosts arteriogenesis in mice", International Journal of Molecular Sciences, vol. 23, no. 15, p. 8454, 2022. https://doi.org/10.3390/ijms23158454
[8] S. Dasari, L. Pereira, A. Reddy, J. Michaels, X. Lu, T. Jacobet al., "Comprehensive proteomic analysis of human cervical−vaginal fluid", Journal of Proteome Research, vol. 6, no. 4, p. 1258-1268, 2007. https://doi.org/10.1021/pr0605419
[9] Y. Kim, K. Kim, H. Oh, S. Lee, & D. Kang, "Quantitative proteomic profiling of cervicovaginal fluid from pregnant women with term and preterm birth", Proteome Science, vol. 19, no. 1, 2021. https://doi.org/10.1186/s12953-021-00171-1
