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Laminin receptor (Lamr) has been given many namesincluding 37 kDa laminin receptor precursor (37-LRP), 67 kDahigh affinity laminin receptor (67-LR), 37 kDa/67 kDa lamininreceptor, p40 ribosome-associated protein and Lamr/p40. It hasbeen reported to be implicated in cell adhesion, mobility, anddifferentiation [1e3]. Many studies of Lamr have employedmammalian models and, apart from cellular functions mentionedabove, it has also been reported to act as a receptor for manyviruses and bacteria [4e10]. Its importance is reflected in therecent attempt to unveil the crystal structure of human Lamr withthe expectation that the knowledge gained will lead to thedevelopment of therapeutics against cancer, neurological diseasesand viral infection [11]. The Lamr sequence in shrimp was firstidentified from the black tiger shrimp (Penaeus monodon) ESTdatabase [12] and later studies revealed that it could bind to theVP1 capsid protein of Taura syndrome virus (TSV) [13]. It was alsoshown to be an essential gene for shrimp viability when knockdownstudies to assess the importance of its interaction with TSVresulted in shrimp mortality even without viral challenge [14].Shrimp proteins functioning as viral receptors or viral bindingproteins have recently drawn much attention as potentialreagents for protection against viral diseases. For example,studies on the use of shrimp proteins to protect against whitespot syndrome virus (WSSV) have been reviewed by [15]. Since
Lamr is recognized as a multifunction protein with a broad range
of binding partners, we decided to test shrimp Lamr for binding
to capsid or envelope proteins of 2 DNA and 3 RNA shrimp viruses
in addition to the RNA virus TSV. Positive results were obtained
for only yellow head virus (YHV) and infectious myonecrosis virus
(IMNV). In addition, laboratory challenge tests revealed that
injection of recombinant Lamr could prevent shrimp mortality
from YHV.
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