Gehring K, Charbit A, Brissaud E, Hofnung M
J Bacteriol. 1987 May;169(5):2103-6. doi: 10.1128/jb.169.5.2103-2106.1987.
We have analyzed eight new phage-resistant missense mutations in lamB. These mutations identify five new amino acid residues essential for phage lambda adsorption. Two mutations at positions 245 and 382 affect residues which were previously identified, but lead to different amino acid changes. Three mutations at residues 163, 164, and 250 enlarge and confirm previously proposed phage receptor sites. Two different mutations at residue 259 and one at 18 alter residues previously suggested as facing the periplasmic face. The mutation at residue 18 implicates for the first time the amino-terminal region of the LamB protein in phage adsorption. The results are discussed in terms of the topology of the LamB protein.
我们分析了lamB基因中的八个新的抗噬菌体错义突变。这些突变确定了五个对λ噬菌体吸附至关重要的新氨基酸残基。位于245和382位的两个突变影响了先前鉴定出的残基，但导致了不同的氨基酸变化。位于163、164和250位的三个突变扩大并证实了先前提出的噬菌体受体位点。位于259位的两个不同突变和位于18位的一个突变改变了先前认为面向周质面的残基。位于18位的突变首次表明LamB蛋白的氨基末端区域参与噬菌体吸附。根据LamB蛋白的拓扑结构对结果进行了讨论。
