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Interaction of merozoite surface protein 2 with lipid membranes
Author(s) -
Lu Chenghui,
Zheng Xue,
Zhang Wei,
Zhao Hongxin,
MacRaild Christopher A.,
Norton Raymond S.,
Zhuang Yonglong,
Wang Junfeng,
Zhang Xuecheng
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13320
Subject(s) - merozoite surface protein , membrane , vesicle , membrane protein , biophysics , chemistry , peripheral membrane protein , cell membrane , peptide , biochemistry , biology , peptide sequence , integral membrane protein , signal peptide , gene
Merozoite surface protein 2 ( MSP 2) is a potential vaccine candidate against malaria, although its functional role is yet to be elucidated. Previous studies showed that MSP 2 can interact with membranes, which may facilitate merozoite invasion into the host cell. The N‐terminal 25 residues of MSP 2 ( MSP 2 1–25 ), which may be aggregated on the merozoite surface, play a key role in the interaction with membranes. Here, we investigated the effects of MSP 2 1–25 –membrane interactions on the conformation and aggregation of MSP 2 1–25 and on membrane integrity, using nanodiscs and small unilamellar vesicles as mimetics of cell membranes. MSP 2 1–25 –membrane interactions induced the peptide to form β‐structure and to aggregate, depending on the lipid composition of the membrane. Nonfibrillar aggregates in turn disrupted the membrane.