Kay W W, Phipps B M, Ishiguro E E, Olafson R W, Trust T J
Can J Biochem Cell Biol. 1984 Nov;62(11):1064-71. doi: 10.1139/o84-137.
Superficial surface layer proteins (A-proteins) were present on diverse isolates of Aeromonas salmonicida which differed both physiologically and in pathogenesis. Three of these proteins were purified directly from the surface of whole cells or from outer membrane preparations. These A-proteins were unusually hydrophobic (45-47%) and of similar but not identical molecular mass (49, 50, and 51 kdaltons). They were nearly identical in amino acid composition and were highly conserved, but not identical with respect to their hydrophobic N-terminal amino acid sequences. These proteins differed, however, with respect to their oligomerization properties, isoelectric forms, and chymotryptic peptide patterns. All three proteins were immunologically closely related and shared surface-exposed immunoreactive peptides with 28 separate isolates.
表面层蛋白(A蛋白)存在于不同的杀鲑气单胞菌分离株中,这些分离株在生理和致病机制上均有所不同。其中三种蛋白可直接从全细胞表面或外膜制剂中纯化得到。这些A蛋白具有异常高的疏水性(45 - 47%),分子量相似但不完全相同(49、50和51千道尔顿)。它们的氨基酸组成几乎相同且高度保守,但疏水性N端氨基酸序列并不相同。然而,这些蛋白在寡聚化特性、等电形式和胰凝乳蛋白酶肽谱方面存在差异。所有这三种蛋白在免疫上密切相关,并且与28个不同的分离株共享表面暴露的免疫反应性肽段。