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Why bacteria derived R-M
nucleic enzymatic peptides are likely efficient therapeutic
molecules for use in the design and development of novel HIV
inhibitory strategies
Wayengera Misaki
Makerere
University, Faculty of Medicine, Kampala, Uganda.
E-mail:
wmisaki@yahoo.com.
Accepted
19 October, 2007 |
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In the past, we have identified, described and isolated over
200 bacteria derived Restriction Modification (R-M) nucleic
enzymatic peptides as efficient therapeutic molecules for
use in the development of novel HIV inhibitory strategies.
In the issuing months of our publications, 3 questions have
been directed to our work; (1) HIV is an RNA virus, thus
restriction peptides are impotent as defense peptides. (2)
HIV genome is encapsulated in nuclear capsid and viral
envelope, making access impossible. (3) Human genome
contains several palindromes recognizable by R-M peptides,
making safety delineation critical. This paper serves to
provide succinct responses to these issues, and highlight
critical strategies being employed in ensuring the
development of safe Microbides and therapeutic vaccines
based on this approach.
Key
words:
Restriction modification (R-M) systems, restriction enzymes
(REases/RNases), methyltranferases (MTases), human
immunodeficiency virus (HIV), immune reconstitution,
probiotic microbicides. |
