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骆驼、牛和人乳过氧化物酶对1型单纯疱疹病毒抗病毒活性的比较分析

Comparative Analysis of the Antiviral Activity of Camel, Bovine, and Human Lactoperoxidases Against Herpes Simplex Virus Type 1.

作者信息

El-Fakharany Esmail M, Uversky Vladimir N, Redwan Elrashdy M

机构信息

Protective and Therapeutic Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute GEBRI, City for Scientific Research and Technology Applications, New Borg El Arab, Alexandria, 21934, Egypt.

Department of Biological Sciences, Faculty of Science, King Abdulaziz University, PO Box 80203, Jeddah, 21589, Saudi Arabia.

出版信息

Appl Biochem Biotechnol. 2017 May;182(1):294-310. doi: 10.1007/s12010-016-2327-x. Epub 2016 Nov 16.

DOI:10.1007/s12010-016-2327-x
PMID:27854033
Abstract

Lactoperoxidase is a milk hemoprotein that acts as a non-immunoglobulin protective protein and shows strong antimicrobial activity. Bovine milk contains about 15 and 7 times higher levels of lactoperoxidase than human colustrum and camel milk, respectively. Human, bovine, and camel lactoperoxidases (hLPO, bLPO, and cLPO, respectively) were purified as homogeneous samples with specific activities of 4.2, 61.3, and 8.7 u/mg, respectively. The optimal working pH was 7.5 (hLPO and bLPO) and 6.5 (cLPO), whereas the optimal working temperature for these proteins was 40 °C. The K of hLPO, cLPO, and bLPO were 17, 16, and 19 mM, and their corresponding V values were 2, 1.7, and 2.7 μmol/min ml. However, in the presence of HO, the K values were 11 mM for hLPO and cLPO and 20 mM for bLPO, while the corresponding V values were 1.17 for hLPO and 1.4 μmol/min ml for cLPO and bLPO. All three proteins were able to inhibit the herpes simplex virus type 1 (HSV-1) in Vero cell line model. The relative antiviral activities were proportional to the protein concentrations. The highest anti-HSV-1 activity was exhibited by bLPO that inhibited the HSV particles at a concentration of 0.5 mg/ml with the relative activity of 100%.

摘要

乳过氧化物酶是一种乳血蛋白,作为一种非免疫球蛋白保护蛋白,具有很强的抗菌活性。牛乳中乳过氧化物酶的含量分别比人初乳和骆驼乳高约15倍和7倍。人、牛和骆驼乳过氧化物酶(分别为hLPO、bLPO和cLPO)被纯化为均一样品,比活性分别为4.2、61.3和8.7 u/mg。最佳工作pH值为7.5(hLPO和bLPO)和6.5(cLPO),而这些蛋白质的最佳工作温度为40℃。hLPO、cLPO和bLPO的Km值分别为17、16和19 mM,其相应的Vmax值分别为2、1.7和2.7 μmol/min ml。然而,在有H2O2存在的情况下,hLPO和cLPO的Km值为11 mM,bLPO的Km值为20 mM,而相应的Vmax值,hLPO为1.17,cLPO和bLPO为1.4 μmol/min ml。在Vero细胞系模型中,所有这三种蛋白质都能够抑制1型单纯疱疹病毒(HSV-1)。相对抗病毒活性与蛋白质浓度成正比。bLPO表现出最高的抗HSV-1活性,其在浓度为0.5 mg/ml时抑制HSV颗粒,相对活性为100%。

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