Savoysky E, Boireau P, Finance C, Laporte J
Laboratoire de Microbiologie Appliquée, Faculté des Sciences Pharmaceutiques et Biologiques, Nancy, France.
Res Virol. 1990 Jul-Aug;141(4):411-25. doi: 10.1016/0923-2516(90)90042-h.
Clones from the bovine enteric coronavirus (F15) cDNA library were cloned in pBR322 and sequenced by the method of Sanger and Coulson. This led to the identification of a sequence of 1,300 bases which contained a single open reading frame of 690 bases yielding a protein having properties of the matrix protein (M). It was comprised of 230 amino acids with a molecular weight of 26,376 Da. It was hydrophobic and had a net charge of +8 at neutral pH. Analysis of its secondary structure could not establish a simple transmembrane arrangement of the amino acids. Comparison of its nucleotide sequence with that of BECV Mebus strain showed only a two-base change resulting in a 100% homology between the two amino acid sequences. Furthermore, a very conserved structure of M appeared on comparison with the Dayoff optimal alignment of MHV-A59, MHV-JHM, TGEV, IBV Beaudette and IBV 6/82M amino acid sequences. As the two strains of BECV, F15 and Mebus present some antigenic differences, this led us to reconsider the role of M in viral antigen specificity. A hypothesis is that, as it seems to possess the necessary information on its transmembrane region, it is an ideal candidate for the viral budding process.
来自牛肠道冠状病毒（F15）cDNA文库的克隆体被克隆到pBR322中，并采用桑格和库尔森的方法进行测序。这导致鉴定出一段1300个碱基的序列，其中包含一个690个碱基的单一开放阅读框，产生一种具有基质蛋白（M）特性的蛋白质。它由230个氨基酸组成，分子量为26376道尔顿。它具有疏水性，在中性pH值下净电荷为+8。对其二级结构的分析未能确定氨基酸的简单跨膜排列。将其核苷酸序列与牛肠道冠状病毒梅布斯株的序列进行比较，结果显示只有两个碱基的变化，导致两个氨基酸序列之间具有100%的同源性。此外，与MHV-A59、MHV-JHM、猪传染性胃肠炎病毒、传染性支气管炎病毒博德特株和传染性支气管炎病毒6/82M的氨基酸序列的戴奥夫最佳比对结果相比，M呈现出非常保守的结构。由于牛肠道冠状病毒的F15和梅布斯这两个毒株存在一些抗原差异，这促使我们重新考虑M在病毒抗原特异性中的作用。一种假设是，由于它似乎在其跨膜区域拥有必要的信息，它是病毒出芽过程的理想候选者。
