Laminin receptor (Lamr) has been given many names
including 37 kDa laminin receptor precursor (37-LRP), 67 kDa
high affinity laminin receptor (67-LR), 37 kDa/67 kDa laminin
receptor, p40 ribosome-associated protein and Lamr/p40. It has
been reported to be implicated in cell adhesion, mobility, and
differentiation [1e3]. Many studies of Lamr have employed
mammalian models and, apart from cellular functions mentioned
above, it has also been reported to act as a receptor for many
viruses and bacteria [4e10]. Its importance is reflected in the
recent attempt to unveil the crystal structure of human Lamr with
the expectation that the knowledge gained will lead to the
development of therapeutics against cancer, neurological diseases
and viral infection [11]. The Lamr sequence in shrimp was first
identified from the black tiger shrimp (Penaeus monodon) EST
database [12] and later studies revealed that it could bind to the
VP1 capsid protein of Taura syndrome virus (TSV) [13]. It was also
shown to be an essential gene for shrimp viability when knockdown
studies to assess the importance of its interaction with TSV
resulted in shrimp mortality even without viral challenge [14].
Shrimp proteins functioning as viral receptors or viral binding
proteins have recently drawn much attention as potential
reagents for protection against viral diseases. For example,
studies on the use of shrimp proteins to protect against white
spot 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.