Bacteriophage lambda receptor site on the Escherichia coli K-12 LamB protein.

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.

[Compression of the cauda equina by osteoarthritic pseudo-spondylolisthesis, with overlying signs of deficit. The possible role of a venous mechanism]. / Compression de la queue de cheval par un pseudo-spondylolisthesis arthrosique, avec signes déficitaires sus-jacents. Rôle possible d'un mécanisme veineux.

The authors report the case of a patient suffering from paraparesis where a venous pathology seemed to be responsible, and the literature is reviewed. A cauda-equina compression by L4/L5 arthrosic pseudo-spondylolisthesis caused troubles of the spinal cord venous drainage, seen at the myelography. There was a neurological deficit above the L4/L5 compression with a psoas and quadriceps deficit. After a L4/L5 laminectomy the neurological signs improved rapidly.