TY - JOUR
T1 - Targeting an antimicrobial effector function in insect immunity as a pest control strategy
AU - Bulmer, Mark S.
AU - Bachelet, Ido
AU - Raman, Rahul
AU - Rosengaus, Rebeca B.
AU - Sasisekharan, Ram
PY - 2009/8/4
Y1 - 2009/8/4
N2 - Insect pests such as termites cause damages to crops and manmade structures estimated at over $30 billion per year, imposing a global challenge for the human economy. Here, we report a strategy for compromising insect immunity that might lead to the development of nontoxic, sustainable pest control methods. Gramnegative bacteria binding proteins (GNBPs) are critical for sensing pathogenic infection and triggering effector responses. We report that termite GNBP-2 (tGNBP-2) shows β(1,3)-glucanase effector activity previously unknown in animal immunity and is a pleiotropic pattern recognition receptor and an antimicrobial effector protein. Termites incorporate this protein into the nest building material, where it functions as a nest-embedded sensor that cleaves and releases pathogenic components, priming termites for improved antimicrobial defense. By means of rational design, we present an inexpensive, nontoxic small molecule glycomimetic that blocks tGNBP-2, thus exposing termites in vivo to accelerated infection and death from specific and opportunistic pathogens. Such a molecule, introduced into building materials and agricultural methods, could protect valuable assets from insect pests.
AB - Insect pests such as termites cause damages to crops and manmade structures estimated at over $30 billion per year, imposing a global challenge for the human economy. Here, we report a strategy for compromising insect immunity that might lead to the development of nontoxic, sustainable pest control methods. Gramnegative bacteria binding proteins (GNBPs) are critical for sensing pathogenic infection and triggering effector responses. We report that termite GNBP-2 (tGNBP-2) shows β(1,3)-glucanase effector activity previously unknown in animal immunity and is a pleiotropic pattern recognition receptor and an antimicrobial effector protein. Termites incorporate this protein into the nest building material, where it functions as a nest-embedded sensor that cleaves and releases pathogenic components, priming termites for improved antimicrobial defense. By means of rational design, we present an inexpensive, nontoxic small molecule glycomimetic that blocks tGNBP-2, thus exposing termites in vivo to accelerated infection and death from specific and opportunistic pathogens. Such a molecule, introduced into building materials and agricultural methods, could protect valuable assets from insect pests.
KW - Gram-negative bacteria binding proteins
KW - Pattern recognition receptor
KW - Social insect immunity
KW - Termites
KW - β(1,3)-glucanase
UR - http://www.scopus.com/inward/record.url?scp=69149088368&partnerID=8YFLogxK
U2 - 10.1073/pnas.0904063106
DO - 10.1073/pnas.0904063106
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
C2 - 19506247
AN - SCOPUS:69149088368
SN - 0027-8424
VL - 106
SP - 12652
EP - 12657
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 31
ER -