TY - JOUR
T1 - LCCL protein complex formation in Plasmodium is critically dependent on LAP1
AU - Tremp, Annie Z.
AU - Sharma, Vikram
AU - Carter, Victoria
AU - Lasonder, Edwin
AU - Dessens, Johannes T.
PY - 2017/6/1
Y1 - 2017/6/1
N2 - Successful sporogony of Plasmodium berghei in vector mosquitoes requires expression of a family of six modular proteins named LCCL lectin domain adhesive-like proteins (LAPs). The LAPs share a subcellular localization in the crystalloid, a unique parasite organelle that forms during ookinete development. Here, LAP interactions in P. berghei were studied using a series of parasite lines stably expressing reporter-tagged LAPs combined with affinity purification and high accuracy label free quantitative mass spectrometry. Our results show that abundant complexes containing LAP1, LAP2 and LAP3 are formed in gametocytes through high avidity interactions. Following fertilization, LAP4, LAP5 and LAP6 are recruited to this complex, a process that is facilitated by LAP1 chiefly through its scavenger receptor cysteine-rich modules. These collective findings provide new insight into the temporal and molecular dynamics of protein complex formation that lead up to, and are required for, crystalloid biogenesis and downstream sporozoite transmission of malaria parasites.
AB - Successful sporogony of Plasmodium berghei in vector mosquitoes requires expression of a family of six modular proteins named LCCL lectin domain adhesive-like proteins (LAPs). The LAPs share a subcellular localization in the crystalloid, a unique parasite organelle that forms during ookinete development. Here, LAP interactions in P. berghei were studied using a series of parasite lines stably expressing reporter-tagged LAPs combined with affinity purification and high accuracy label free quantitative mass spectrometry. Our results show that abundant complexes containing LAP1, LAP2 and LAP3 are formed in gametocytes through high avidity interactions. Following fertilization, LAP4, LAP5 and LAP6 are recruited to this complex, a process that is facilitated by LAP1 chiefly through its scavenger receptor cysteine-rich modules. These collective findings provide new insight into the temporal and molecular dynamics of protein complex formation that lead up to, and are required for, crystalloid biogenesis and downstream sporozoite transmission of malaria parasites.
KW - Crystalloid organelle
KW - LC/MS/MS
KW - LCCL
KW - Transmission blockade
UR - http://www.scopus.com/inward/record.url?scp=85018800111&partnerID=8YFLogxK
UR - https://pearl.plymouth.ac.uk/handle/10026.1/9093
U2 - 10.1016/j.molbiopara.2017.04.005
DO - 10.1016/j.molbiopara.2017.04.005
M3 - Article
C2 - 28414172
AN - SCOPUS:85018800111
SN - 0166-6851
VL - 214
SP - 87
EP - 90
JO - Molecular and Biochemical Parasitology
JF - Molecular and Biochemical Parasitology
ER -
