Why whey? Camel whey protein as a new dietary approach to the management of free radicals and for the treatment of different health disorders

Document Type : Review Article


1 Zoology Department, Faculty of Science, Assiut University, 71516 Assiut, Egypt

2 Laboratory of Immunology & Molecular Physiology, Zoology Department, Faculty of Science, Assiut University, 71516 Assiut, Egypt

3 Animal Health Research Institute, Assiut Branch. Assiut, Egypt

4 Department of Radiation Biology, National Centre for Radiation Research and Technology (NCRRT), Atomic Energy Authority, Egypt

5 Department of Biology, Faculty of Arts and Sciences, Nigde University, Nigde, Turkey


The balance between free radicals and antioxidants is an important factor for maintaining health and slowing disease progression. The use of antioxidants, particularly natural antioxidants, has become an important strategy for dealing with this cause of widespread diseases. Natural antioxidants have been used as therapeutic tools against many diseases because they are safe, effective, and inexpensive and are among the most commonly used adjuvants in the treatment of several diseases. Camel whey protein (CWP) is considered a strong natural antioxidant because it decreases oxidative stress, enhances immune system function, and increases glutathione levels. The structure of CWP is very similar to that of other types of whey protein from different types of milk. CWP contains many components, such as lactoferrin (LF), lactalbumin, lactoglobulins, lactoperoxidase, and lysozyme, and is rich in immunoglobulins. However, in contrast to other WPs, CWP lacks β-lactoglobulin, the main cause of milk allergies in children. The components of CWP have many beneficial effects, including stimulation of both innate and adaptive immunity and anti-inflammatory, anticancer, antibacterial, and antiviral activities. Recently, it has been shown that CWP and its unique components can facilitate the treatment of impaired diabetic wound healing. However, the molecular mechanisms underlying the protective effects of CWP in human and other animal disorders are not fully understood. Therefore, the current review presents a concise summary of the scientific evidence of the beneficial effects of CWP to support its therapeutic use in disease treatment and nutritional intervention.


1.Ebaid H, Badr G, Metwalli A. Immunoenhancing property of dietary un-denatured whey protein derived from three camel breeds in mice. Biologia 2012; 67:425-433.
2.Badr G, Badr BM, Mahmoud MH, Mohany M, Rabah DM, Garraud O. Treatment of diabetic mice with undenatured whey protein accelerates the wound healing process by enhancing the expression of mip-1α, mip-2, kc, cx3cl1 and tgf-β in wounded tissue. BMC Immunol 2012; 13:32.
3.Badr G. Camel whey protein enhances diabetic wound healing in a streptozotocin-induced diabetic mouse model: The critical role of β-defensin-1,-2 and-3. Lipids Health Dis 2013; 12:1.
4.Badr G. Supplementation with undenatured whey protein during diabetes mellitus improves the healing and closure of diabetic wounds through the rescue of functional long-lived wound macrophages. Cell Physiol Biochem 2012; 29:571-582.
5.Badr G, Mohany M, Metwalli A. Effects of undenatured whey protein supplementation on cxcl12-and ccl21-mediated b and t cell chemotaxis in diabetic mice. Lipids Health Dis 2011; 10:1.
6.Badr G, Ebaid H, Mohany M, Abuelsaad AS. Modulation of immune cell proliferation and chemotaxis towards cc chemokine ligand (ccl)-21 and cxc chemokine ligand (cxcl)-12 in undenatured whey protein-treated mice. J Nutr Biochem 2012; 23:1640-1646.
7.Mohany M, Badr BM, Mahmoud MH, Garraud O, Badr G. Un-denatured whey protein expedites wound healing in diabetic mice model by enhancing the expression of beta-defensin 2, 3 and vascular endothelial growth factor (vegf) in the wounded tissue. Afr J Microbiol Res 2012; 6;2137-2144.
8.Power O, Jakeman P, FitzGerald R. Antioxidative peptides: Enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides. Amino Acids 2013; 44:797-820.
9.Marshall K. Therapeutic applications of whey protein. Altern Med Rev 2004; 9:136-156.
10.El-Hatmi H, Girardet JM, Gaillard JL, Yahyaoui MH, Attia H. Characterisation of whey proteins of camel (camelus dromedarius) milk and colostrum. Small Rumin Res 2007;70:267-271.
11.Salami M, Moosavi-Movahedi AA, Ehsani MR, Yousefi R, Haertlé T, Chobert JM, et al. Improvement of the antimicrobial and antioxidant activities of camel and bovine whey proteins by limite proteolysis. J Agric Food Chem. 2010; 58:3297-3302.
12.Abdel-Aziem SH, Hassan AM, Abdel-Wahhab MA. Dietary supplementation with whey protein and ginseng extract counteracts oxidative stress and DNA damage in rats fed an aflatoxin-contaminated diet. Mutat Res Genet Toxicol Environ Mutagen 2011; 723:65-71.
13.Sousa GT, Lira FS, Rosa JC, de Oliveira EP, Oyama LM, Santos RV, et al. Dietary whey protein lessens several risk factors for metabolic diseases: A review. Lipids Health Dis 2012; 11:1-9.
14.Ebaid H, Ahmed OM, Mahmoud AM, Ahmed RR. Limiting prolonged inflammation during proliferation and remodeling phases of wound healing in streptozotocin-induced diabetic rats supplemented with camel undenatured whey protein. BMC Immunol 2013; 14:1-13.
15.Khaskheli M, Arain M, Chaudhry S, Soomro A, Qureshi T. Physico-chemical quality of camel milk. J Agri Soc Sci 2005; 2:164-166.
16.Kappeler SR, Heuberger C, Farah Z, Puhan Z. Expression of the peptidoglycan recognition protein, pgrp, in the lactating mammary gland. J Dairy Sci 2004; 87:2660-2668.
17.Elagamy EI. Effect of heat treatment on camel milk proteins with respect to antimicrobial factors: A comparison with cows' and buffalo milk proteins. Food Chem 2000; 68:227-232.
18.Lucas DO. Breakthrough technology produces concentrated whey protein with bioactive immunoglobulins. Clin Nutr Insight 1999; 6:1-4.
19.Laleye L, Jobe B, Wasesa A. Comparative study on heat stability and functionality of camel and bovine milk whey proteins. J Dairy Sci 2008; 91:4527-4534.
20.Hinz K, O'Connor PM, Huppertz T, Ross RP, Kelly AL. Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk. J Dairy Sci 2012; 79:185-191.
21.El-Agamy EI, Nawar M, Shamsia SM, Awad S, Haenlein GF. Are camel milk proteins convenient to the nutrition of cow milk allergic children? Small Rumin Res 2009; 82;1-6.
22.Kappeler S, Farah Z, Puhan Z. Alternative splicing of lactophorin mrna from lactating mammary gland of the camel (camelus dromedarius). J Dairy Sci 1999; 82:2084-2093.
23.Cohen MS, Britigan BE, French M, Bean K. Preliminary observations on lactoferrin secretion in human vaginal mucus: Variation during the menstrual cycle, evidence of hormonal regulation, and implications for infection with neisseria gonorrhoeae. Am J Obstet Gynecol 1987; 157:1122-1125.
24.Harmsen MC, Swart PJ, de Béthune MP, Pauwels R, De Clercq E, Meijer DK. Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro. J  Infect Dis 1995; 172:380-388.
25.Sanchez L, Calvo M, Brock JH. Biological role of lactoferrin. Arch Dis Child 1992; 67:657.
26.Conesa C, Sánchez L, Rota C, Pérez MD, Calvo M, Farnaud S, et al. Isolation of lactoferrin from milk of different species: Calorimetric and antimicrobial studies. Comp Biochem Physiol B Biochem Mol Biol 2008; 150:131-139.
27.Gauthier SF, Pouliot Y, Saint-Sauveur D. Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. Int Dairy J 2006; 16:1315-1323.
28.Rusu D, Drouin R, Pouliot Y, Gauthier S, Poubelle PE. A bovine whey protein extract stimulates human neutrophils to generate bioactive il-1ra through a nf-κb-and mapk-dependent mechanism. J Nutr 2010; 140:382-391.
29.Micke P, Beeh K, Schlaak J, Buhl R. Oral supplementation with whey proteins increases plasma glutathione levels of hiv‐infected patients. Eur J Clin Invest 2001; 31:171-178.
30.Krissansen GW. Emerging health properties of whey proteins and their clinical implications. J Am Coll Nutr 2007; 26:713-723.
31.Beaulieu J, Dupont C, Lemieux P. Whey proteins and peptides: Beneficial effects on immune health. 1st ed.Springer; 2006.
32.Loss G, Apprich S, Waser M, Kneifel W, Genuneit J, Büchele G, et al. The protective effect of farm milk consumption on childhood asthma and atopy: The gabriela study. J Allergy Clin Immunol 2011; 128;766-773. e764.
33.Castro G, Maria D, Bouhallab S, Sgarbieri V. In vitro impact of a whey protein isolate (wpi) and collagen hydrolysates (chs) on b16f10 melanoma cells proliferation. J Dermatol Sci 2009; 56:51-57.
34.Ebaid H, Salem A, Sayed A, Metwalli A. Whey protein enhances normal inflammatory responses during cutaneous wound healing in diabetic rats. Lipids Health Dis 2011; 10:1.
35.Ebaid H. Promotion of immune and glycaemic functions in streptozotocin-induced diabetic rats treated with un-denatured camel milk whey proteins. Nutr Metab (Lond) 2014; 11:31.
36.Ebaid H. Neutrophil depletion in the early inflammatory phase delayed cutaneous wound healing in older rats: Improvements due to the use of un-denatured camel whey protein. Diagn Pathol 2014; 9:46.
37.Walzem R, Dillard C, German J. Whey components: Millennia of evolution create functionalities for mammalian nutrition: What we know and what we may be overlooking. Crit Rev Food Sci Nutr 2002; 42:353-375.
38.Low PPL, Rutherford KJ, Gill HS, Cross ML. Effect of dietary whey protein concentrate on primary and secondary antibody responses in immunized BALB/CMice. Int Immunopharmacol 2003; 3:393-401.
39.Faloon PW, Chou DHC, Forbeck EM, Walpita D, Morgan B, Buhrlage S, et al. Identification of small molecule inhibitors that suppress cytokine-induced apoptosis in human pancreatic islet cells. Probe Reports from the NIH Molecular Libraries Program;2011.
40.Bounous G, Batist G, Gold P. Immunoenhancing property of dietary whey protein in mice: Role of glutathione. Clin Invest Med 1989; 12:154-161.
41.Belokrylov G, Popova OY, Molchanova I, Sorochinskaya E, Anokhina V. Peptides and their constituent amino acids influence the immune response and phagocytosis in different ways. Int J Immunopharmacol 1992; 14:1285-1292.
42.Kawasaki H. Comparative studies on proteodermatan sulfate of bovine gastrointestinal tract. Tohoku J Exp Med. 1993;171:255-266.
43.Marchetti M, Pisani S, Antonini G, Valenti P, Seganti L, Orsi N. Metal complexes of bovine lactoferrin inhibit in vitro replication of herpes simplex virus type 1 and 2. Biometals 1998; 11:89-94.
44.Wong CW, Watson DL. Immunomodulatory effects of dietary whey proteins in mice. J Dairy Res 1995; 62:359-368.
45.Machnicki M, Zimecki M, Zagulski T. Lactoferrin regulates the release of tumour necrosis factor alpha and interleukin 6 in vivo. Int J Exp Pathol 1993; 74:433.
46.Ögünç V, Manukyan Cingi, Eksioglu-Demiralp, Aktan Ö, Yalçın S. Dietary whey supplementation in experimental models of wound healing. Int J Vitam Nutr Res 2008; 78:70-73.
47.Ajarem J, Allam AA, Ebaid H, Maodaa SN, AL-Sobeai SM, Rady AM, et al. Neurochemical, structural and neurobehavioral evidence of neuronal protection by whey proteins in diabetic albino mice. Behav Brain Funct 2015; 11:1.
48.Takamiya M, Fujita S, Saigusa K, Aoki Y. Simultaneous detections of 27 cytokines during cerebral wound healing by multiplexed bead-based immunoassay for wound age estimation. J Neurotrauma 2007; 24:1833-1844.
49.Lin Q, Fang D, Fang J, Ren X, Yang X, Wen F, e al. Impaired wound healing with defective expression of chemokines and recruitment of myeloid cells in tlr3-deficient mice. J Immunol 2011; 186:3710-3717.
50.Mori R, Kondo T, Ohshima T, Ishida Y, Mukaida N. Accelerated wound healing in tumor necrosis factor receptor p55-deficient mice with reduced leukocyte infiltration. FASEB J 2002; 16;963-974.
51.Black E, Vibe-Petersen J, Jorgensen LN, Madsen SM, Ågren MS, Holstein PE, et al. Decrease of collagen deposition in wound repair in type 1 diabetes independent of glycemic control. Arch Surg 2003; 138:34-40.
52.Zhang Z, Zhao M, Wang J, Ding Y, Dai X, Li Y. Oral administration of skin gelatin isolated from chum salmon (oncorhynchus keta) enhances wound healing in diabetic rats. Mar Drugs 2011; 9:696-711.
53.Mahmoud MH, Badr G, El Shinnawy NA. Camel whey protein improves lymphocyte function and protects against diabetes in the offspring of diabetic mouse dams. Int J Immunopathol Pharmacol 2016; 29:632-646.
54.Habib HM, Ibrahim WH, Schneider-Stock R, Hassan HM. Camel milk lactoferrin reduces the proliferation of colorectal cancer cells and exerts antioxidant and DNA damage inhibitory activities. Food Chem 2013; 141:148-152.
55.Papenburg R, Bounous G, Fleiszer D, Gold P. Dietary milk proteins inhibit the development of dimethylhydrazine-induced malignancy. Tumour Biol 1990; 11;129-136.
56.Bounous G, Batist G, Gold P. Whey proteins in cancer prevention. Cancer Lett. 1991; 57:91-94.
57.McIntosh GH, Regester GO, Le Leu RK, Royle PJ, Smithers GW. Dairy proteins protect against dimethylhydrazine-induced intestinal cancers in rats. J Nutr 1995; 125:809-816.
58.Hakkak R, Korourian S, Shelnutt SR, Lensing S, Ronis MJ, Badger TM. Diets containing whey proteins or soy protein isolate protect against 7,12-dimethylbenz(a)anthracene-induced mammary tumors in female rats. Cancer Epidemiol Biomarkers Prev 2000; 9:113-117.
59.Bounous G. Whey protein concentrate (wpc) and glutathione modulation in cancer treatment. Anticancer Res 2000; 20:4785-4792.
60.Hakkak R, Korourian S, Ronis MJ, Johnston JM, Badger TM. Dietary whey protein protects against azoxymethane-induced colon tumors in male rats. Cancer Epidemiol Biomarkers Prev 2001; 10:555-558.
61.Zimecki M, Wlaszczyk A, Wojciechowski R, Dawiskiba J, Kruzel, M. Lactoferrin regulates the immune responses in post-surgical patients. Arch Immunol Ther Exp 2001; 49:325-333.
62.Guimont C, Marchall E, Girardet JM, Linden G. Biologically active factors in bovine milk and dairy byproducts: Influence on cell culture. Crit Rev Food Sci Nut 1997; 37:393-410.
63.Morales A, Miranda M, Sanchez-Reyes A, Biete A, Fernandez-Checa JC. Oxidative damage of mitochondrial and nuclear DNA induced by ionizing radiation in human hepatoblastoma cells. Int J Radiat Oncol Biol Phys 1998; 42:191-203.
64.Friesen C, Kiess Y, Debatin KM. A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells. Cell Death Differ 2004; 1:S73-85.
65.Nukumi N, Iwamori T, Kano K, Naito K, Tojo H. Reduction of tumorigenesis and invasion of human breast cancer cells by whey acidic protein (wap). Cancer Lett 2007; 252:65-74.
66.Tsuda H, Miyamoto T. Angiotensin i‐converting enzyme inhibitory peptides in skim milk fermented with lactobacillus helveticus 130b4 from camel milk in inner mongolia, china. J Sci Food Agric 2008; 88:2688-2692.
67.Smith CG, Vane JR. The discovery of captopril. FASEB J 2003; 17:788-789.
68.AlhajOA KA, Peters A. The effect of bifid bacterium lactis and trypsin on cholesterol international food and health innovation conference. Malmö, Sweden: Skåne Food Innovation Network;2006.
69.López-Fandiño R, Otte J, Van Camp J. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ace-inhibitory activity. Int Dairy J 2006; 16:1277-1293.
70.Li H, Papadopoulos V. Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern 1. Endocrinol 1998; 139:4991-4997.
71.Seelig A, Seelig J. In interaction of drugs and peptides with the lipid membrane.Alfred Benzon Symposium, Munksgaard; 1996.p.184-191.
72.Agrawal R, Budania S, Sharma P, Gupta R, Kochar D, Panwar R, Sahani M. Zero prevalence of diabetes in camel milk consuming raica community of north-west rajasthan, india. Diabetes Res Clin Pract Supp 2007; 76:290-296.
73.Agrawal RP, Saran S, Sharma P, Gupta RP, Kochar DK, Sahani MS. Effect of camel milk on residual β-cell function in recent onset type 1 diabetes. Diabetes Res Clin Pract  2007; 77:494-495.
74.Sanz Fernandez MV, Pearce SC, Mani V, Gabler NK, Metzger L, Patience JF, Rhoads RP, et al. Effects of dairy products on intestinal integrity in heat-stressed pigs. Temperature 2014; 1;128-134.
75.El Sayed I, Ruppanner R, Ismail A, Champagne CP, Assaf R. Antibacterial and antiviral activity of camel milk protective proteins. J Dairy Res 1992; 59:169-175.
76.Ochoa TJ, Cleary TG. Effect of lactoferrin on enteric pathogens. Biochimie 2009; 91:30-34.
77.Benkerroum N. Antimicrobial activity of lysozyme with special relevance to milk. Afric J Biotechnol 2008;7.
78.Konuspayeva G, Faye B, Loiseau G, Levieux D. Lactoferrin and immunoglobulin contents in camel's milk (camelus bactrianus, camelus dromedarius, and hybrids) from kazakhstan. J Dairy Sci 2007; 90:38-46.
79.Hara K, Ikeda M, Saito S, Matsumoto S, Numata K, Kato N, et al. Lactoferrin inhibits hepatitis b virus infection in cultured human hepatocytes. Hepatol Res. 2002; 24:228-235.
80.Redwan ERM, Tabll A. Camel lactoferrin markedly inhibits hepatitis c virus genotype 4 infection of human peripheral blood leukocytes. J Immunoassay Immunochem 2007; 28:267-277.
81.Håkansson A, Svensson M, Mossberg AK, Sabharwal H, Linse S, Lazou I, et al. A folding variant of α‐lactalbumin with bactericidal activity against streptococcus pneumoniae. Mol Microbiol 2000; 35:589-600.
82.Benkerroum N, Mekkaoui M, Bennani N, Hidane K. Antimicrobial activity of camel's milk against pathogenic strains of escherichia coli and listeria monocytogenes. Int J Dairy Technol 2004; 57:39-43.
83.Jrad Z, El Hatmi H, Adt I, Girardet JM, Cakir-Kiefer C, Jardin J, et al. Effect of digestive enzymes on antimicrobial, radical scavenging and angiotensin i-converting enzyme inhibitory activities of camel colostrum and milk proteins. Dairy Sci Technol 2014; 94:205-224.
84.EL-Fakharany EM, Abedelbaky N, Haroun BM, Sánchez L, Redwan NA, Redwan EM. Anti-infectivity of camel polyclonal antibodies against hepatitis c virus in huh7. 5 hepatoma. Virol J 2012; 9:1.
85.Esmail ME, Ashraf T, El WA, Bakry MH, El-Rashdy MR. Potential activity of camel milk-amylase and lactoferrin against hepatitis c virus infectivity in hepg2 and lymphocytes. Hepat Mon 2008; 2008:101-109.
86.Liao Y, El-Fakkarany E, Lönnerdal B, Redwan EM. Inhibitory effects of native and recombinant full-length camel lactoferrin and its n and c lobes on hepatitis c virus infection of huh7. 5 cells. J Med Microbiol 2012; 61:375-383.
87.Arnold RR, Russell JE, Champion WJ, Brewer M, Gauthier JJ. Bactericidal activity of human lactoferrin: Differentiation from the stasis of iron deprivation. Infect Immun 1982; 35:792-799.
88.Crouch S, Slater K, Fletcher J. Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin. Blood 1992; 80:235-240.
89.Hashizume S, Kuroda K, Murakami H. Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium. Biochim Biophys Acta (BBA)-Mol Cell Res 1983; 763:377-382.
90.Legrand D, Pierce A, Elass E, Carpentier M, Mariller C, Mazurier J. Lactoferrin structure and functions. In Bioactive components of milk, Springer; 2008.p.163-194.
91.Redwan EM, EL-Fakharany EM, Uversky VN, Linjawi MH. Screening the anti infectivity potentials of native n-and c-lobes derived from the camel lactoferrin against hepatitis c virus. BMC Complement Altern Med 2014; 14:1.
92.EL-Fakharany EM, Sánchez L, Al-Mehdar HA, Redwan EM. Effectiveness of human, camel, bovine and sheep lactoferrin on the hepatitis c virus cellular infectivity: Comparison study. Virol J 2013; 10:1.
93.Holt LJ, Herring C, Jespers LS, Woolven BP, Tomlinson IM. Domain antibodies: Proteins for therapy. Trends Biotechnol 2003; 21:484-490.
94.Bonkovsky HL, Banner BF, Rothman AL. Iron and chronic viral hepatitis. Hepatology 1997; 25:759-768.
95.Farinati F, Cardin R, De Maria N, Della Libera G, Marafin C, Lecis E, et al. Iron storage, lipid peroxidation and glutathione turnover in chronic anti-hcv positive hepatitis. J Hepatol 1995; 22:449-456.
96.Saltanat H, Li H, Xu Y, Wang J, Liu F, Geng X. [the influences of camel milk on the immune response of chronic hepatitis b patients]. Xi bao yu fen zi mian yi xue za zhi= Chinese J Cell Mol Immunol 2009; 25:431-433.
97.Ikeda M, Sugiyama K, Tanaka T, Tanaka K, Sekihara H, Shimotohno K, et al. Lactoferrin markedly inhibits hepatitis c virus infection in cultured human hepatocytes. Biochem Biophys Res Commun 1998; 245:549-553.
98.Berkhout B, van Wamel JL, Beljaars L, Meijer DK, Visser S, Floris R. Characterization of the anti-hiv effects of native lactoferrin and other milk proteins and protein-derived peptides. Antiviral Res 2002; 55:341-355.
99.Pietrantoni A, Di Biase AM, Tinari A, Marchetti M, Valenti P, Seganti L, et al. Bovine lactoferrin inhibits adenovirus infection by interacting with viral structural polypeptides. Antimicrob Agents Chemother 2003; 47:2688-2691.
100.Van der Strate B, Beljaars L, Molema G, Harmsen M, Meijer D. Antiviral activities of lactoferrin. Antiviral Res 2001; 52:225-239.
101.Copreni E, Castellani S, Palmieri L, Penzo M, Conese M. Involvement of glycosaminoglycans in vesicular stomatitis virus g glycoprotein pseudotyped lentiviral vector‐mediated gene transfer into airway epithelial cells. J Gene Med 2008; 10:1294-1302.
102.Leistner CM, Gruen‐Bernhard S, Glebe D. Role of glycosaminoglycans for binding and infection of hepatitis b virus. Cell Microbiol 2008; 10:122-133.
103.Spear PG. Herpes simplex virus: Receptors and ligands for cell entry. Cell Microbiol 2004; 6;401-410.
104.Sapp M, Bienkowska‐Haba M. Viral entry mechanisms: Human papillomavirus and a long journey from extracellular matrix to the nucleus. FEBS J 2009; 276:7206-7216.
105.Akhtar J, Shukla D. Viral entry mechanisms: Cellular and viral mediators of herpes simplex virus entry. FEBS J 2009; 276:7228-7236.
106.Cocquerel L, Voisset C, Dubuisson J. Hepatitis c virus entry: Potential receptors and their biological functions. J Gen Virol 2006; 87:1075-1084.
107.Schulze A, Gripon P, Urban S. Hepatitis b virus infection initiates with a large surface protein–dependent binding to heparan sulfate proteoglycans. Hepatology 2007; 46:1759-1768.
108.Belting M. Heparan sulfate proteoglycan as a plasma membrane carrier. Trends Biocheml Sci 2003; 28:145-151.
109.Burckhardt CJ, Greber UF. Virus movements on the plasma membrane support infection and transmission between cells. PLoS Pathog 2009; 5:e1000621.
110.Selinka HC, Giroglou T, Sapp M. Analysis of the infectious entry pathway of human papillomavirus type 33 pseudovirions. Virology 2002; 299:279-287.
111.Beleid R, Douglas D, Kneteman N, Kaur K. Helical peptides derived from lactoferrin bind hepatitis c virus envelope protein e2. Chem Biol Drug Des 2008; 72:436-443.
112.Gifford JL, Ishida H, Vogel HJ. Structural characterization of the interaction of human lactoferrin with calmodulin. PLoS One 2012; 7:e51026.
113.Lin Q, Fang D, Hou X, Le Y, Fang J, Wen F, et al. Hcv peptide (c5a), an amphipathic α-helical peptide of hepatitis virus c, is an activator of n-formyl peptide receptor in human phagocytes. J Immunol 2011; 186;2087-2094.
114.Zhang J, Mulvenon A, Makarov E, Wagoner J, Knibbe J, Kim JO, et al. Antiviral peptide nanocomplexes as a potential therapeutic modality for hiv/hcv co-infection. Biomaterials 2013; 34:3846-3857.
115.Martin F, Volpari C, Steinkuhler C, Dimasi N, Brunetti M, Biasiol G, et al. Affinity selection of a camelized v (h) domain antibody inhibitor of hepatitis c virus ns3 protease. Protein Engin 1997; 10:607-614.
116.Lauwereys M, Ghahroudi MA, Desmyter A, Kinne, J, Hölzer W, De Genst E, et al. Potent enzyme inhibitors derived from dromedary heavy‐chain antibodies. EMBO J 1998; 17:3512-3520.
117.Davies MJ, Hawkins CL, Pattison DI, Rees MD. Mammalian heme peroxidases: From molecular mechanisms to health implications. Antioxid Redox Signal 2008; 10:1199-1234.
118.Redwan EM, Almehdar HA, EL-Fakharany EM, Baig AWK, Uversky VN. Potential antiviral activities of camel, bovine, and human lactoperoxidases against hepatitis c virus genotype 4. RSC Adv 2015; 5:60441-60452.
119.Courtois P, Van Beers D, De Foor M, Mandelbaum I, Pourtois M. Abolition of herpes simplex cytopathic effect after treatment with peroxidase generated hypothiocyanite. J Biol Buccale 1990; 18:71-74.
120.Mikola H, Waris M, Tenovuo J. Inhibition of herpes simplex virus type 1, respiratory syncytial virus and echovirus type 11 by peroxidase-generated hypothiocyanite. Antiviral Res 1995; 26:161-171.
121.Yamaguchi Y, Semmel M, Stanislawski L, Strosberg A, Stanislawski M. Virucidal effects of glucose oxidase and peroxidase or their protein conjugates on human immunodeficiency virus type 1. Antimicrob Agents Chemother 1993; 37:26-31.