Abstract:
:Using simple design and selective pressure, we have evolved an artificial M13 bacteriophage coat protein. M13 coat proteins first reside in the bacterial inner membrane and subsequently surround the DNA core of the assembled virus. The artificial coat protein (ACP) was designed and evolved to mimic both functions of the natural M13 coat proteins, but with an inverted orientation. ACP is a non-functional coat protein because it is not required for the production of phage particles. Instead, it incorporates into a phage coat which still requires all the natural coat proteins for structural integrity. In contrast with other M13 coat proteins, which can display polypeptides as amino-terminal fusions, ACP permits the carboxy-terminal display of large polypeptides. The results suggest that viruses can co-opt host membrane proteins to acquire new coat proteins and thus new functions. In particular, M13 bacteriophage can be engineered for new functions, such as carboxy-terminal phage display.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Weiss GA,Sidhu SSdoi
10.1006/jmbi.2000.3845keywords:
subject
Has Abstractpub_date
2000-06-30 00:00:00pages
213-9issue
1eissn
0022-2836issn
1089-8638pii
S0022-2836(00)93845-2journal_volume
300pub_type
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