Llama antibodies against a lactococcal protein located at the tip of the phage tail prevent phage infection

被引:59
作者
De Haard, HJW
Bezemer, S
Ledeboer, AM
Müller, WH
Boender, PJ
Moineau, S
Coppelmans, MC
Verkleij, AJ
Frenken, LGJ
Verrips, CT
机构
[1] Unilever Res Vlaardingen, Dept Biotechnol, NL-3133 AT Vlaardingen, Netherlands
[2] Biotechnol Applicat Ctr, NL-1411 GP Naarden, Netherlands
[3] Univ Utrecht, EMSA, Dept Mol Cell Biol, NL-3584 CH Utrecht, Netherlands
[4] Biotechnol Res Unit, NL-5281 RM Boxtel, Netherlands
[5] Univ Laval, Dept Biochem & Microbiol, Ste Foy, PQ G1K 7P4, Canada
关键词
D O I
10.1128/JB.187.13.4531-4541.2005
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Bacteriophage p2 belongs to the most prevalent lactococcal phage group (936) responsible for considerable losses in industrial production of cheese. Immunization of a llama with bacteriophage p2 led to higher titers of neutralizing heavy-chain antibodies (i.e., devoid of light chains) than of the classical type of immunoglobulins. A panel of p2-specific single-domain antibody fragments was obtained using phage display technology, from which a group of potent neutralizing antibodies were identified. The antigen bound by these antibodies was identified as a protein with a molecular mass of 30 kDa, homologous to open reading frame 18 (ORF18) of phage sk1, another 936-like phage for which the complete genomic sequence is available. By the use of immunoelectron microscopy, the protein is located at the tip of the tail of the phage particle. The addition of purified ORF18 protein to a bacterial culture suppressed phage infection. This result and the inhibition of cell lysis by anti-ORF18 protein antibodies support the conclusion that the ORF18 protein plays a crucial role in the interaction of bacteriophage p2 with the surface receptors of Lactococcus lactis.
引用
收藏
页码:4531 / 4541
页数:11
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