Notariale Rosaria, Basile Adriana, Montana Elena, Romano Nunzia Colonna, Cacciapuoti Maria Grazia, Aliberti Francesco, Gesuele Renato, De Ruberto Francesca, Sorbo Sergio, Tenore Gian Carlo, Guida Marco, Good Katrina V, Ausió Juan, Piscopo Marina
Dipartimento di Biologia, Università degli Studi di Napoli Federico II. Napoli, Italy.
Ce.S.M.A, Section of Microscopy, University of Naples Federico II, Complesso Univ. Monte Sant'Angelo, Via Cinthia 4, 80126 Napoli, Italy.
Acta Biochim Pol. 2018 Nov 17;65(4):585-594. doi: 10.18388/abp.2018_2638.
The major acid-soluble protein components of the mussel Mytilus galloprovincialis sperm chromatin consist of the protamine-like proteins PL-II, PL-III and PL-IV, an intermediate group of sperm nuclear basic proteins between histones and protamines. The aim of this study was to investigate the bactericidal activity of these proteins since, to date, there are reports on bactericidal activity of protamines and histones, but not on protamine-like proteins. We tested the bactericidal activity of these proteins against Gram-positive bacteria: Enterococcus faecalis and two different strains of Staphylococcus aureus, as well as Gram-negative bacteria: Proteus mirabilis, Proteus vulgaris, Pseudomonas aeruginosa, Salmonella typhmurium, Enterobacter aerogenes, Enterobacter cloacae, and Escherichia coli. Clinical isolates of the same bacterial species were also used to compare their sensitivity to these proteins. The results show that Mytilus galloprovincialis protamine-like proteins exhibited bactericidal activity against all bacterial strains tested with different minimum bactericidal concentration values, ranging from 15.7 to 250 µg/mL. Furthermore, these proteins were active against some bacterial strains tested that are resistant to conventional antibiotics. These proteins showed very low toxicity as judged by red blood cell lysis and viability MTT assays and seem to act both at the membrane level and within the bacterial cell. We also tested the bactericidal activity of the product obtained from an in vitro model of gastrointestinal digestion of protamine-like proteins on a Gram-positive and a Gram-negative strain, and obtained the same results with respect to undigested protamine-like proteins on the Gram-positive bacterium. These results provide the first evidence of bactericidal activity of protamine-like-proteins.
地中海贻贝精子染色质的主要酸溶性蛋白质成分包括类鱼精蛋白PL-II、PL-III和PL-IV,它们是介于组蛋白和鱼精蛋白之间的一组精子核碱性蛋白。本研究的目的是探究这些蛋白质的杀菌活性,因为迄今为止,有关于鱼精蛋白和组蛋白杀菌活性的报道,但没有关于类鱼精蛋白杀菌活性的报道。我们测试了这些蛋白质对革兰氏阳性菌粪肠球菌和两种不同菌株的金黄色葡萄球菌的杀菌活性,以及对革兰氏阴性菌奇异变形杆菌、普通变形杆菌、铜绿假单胞菌、鼠伤寒沙门氏菌、产气肠杆菌、阴沟肠杆菌和大肠杆菌的杀菌活性。还使用了相同细菌种类的临床分离株来比较它们对这些蛋白质的敏感性。结果表明,地中海贻贝类鱼精蛋白对所有测试的细菌菌株均表现出杀菌活性,其最小杀菌浓度值不同,范围为15.7至250μg/mL。此外,这些蛋白质对一些测试的对传统抗生素耐药的细菌菌株也有活性。通过红细胞裂解和MTT活力测定判断,这些蛋白质的毒性非常低,并且似乎在膜水平和细菌细胞内均起作用。我们还测试了从类鱼精蛋白的胃肠道消化体外模型获得的产物对一株革兰氏阳性菌和一株革兰氏阴性菌的杀菌活性,对于革兰氏阳性菌,得到了与未消化的类鱼精蛋白相同的结果。这些结果提供了类鱼精蛋白具有杀菌活性的首个证据。