Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils.
Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils.
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DOI：
10.1016/j.molbiopara.2009.03.012
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发表时间：
2009-08
影响因子：
1.5
通讯作者：
Anders, Robin F.
中科院分区：
文献类型：
--
作者：
Adda, Christopher G.;Murphy, Vince J.;Sunde, Margaret;Waddington, Lynne J.;Schloegel, Jesse;Talbo, Gert H.;Vingas, Kleo;Kienzle, Vivian;Masciantonio, Rosella;Howlett, Geoffrey J.;Hodder, Anthony N.;Foley, Michael;Anders, Robin F.
几种裂殖子表面蛋白正在被评估为恶性疟原虫疫苗的潜在成分，恶性疟原虫是人类最严重的疟疾形式的原因。其中一种蛋白质，裂殖子表面蛋白2(MSP2)，是一种异常亲水性的蛋白质，含有串联序列重复序列，这是内在非结构蛋白的特征。一系列物理化学研究证实，MSP2的重组形式在很大程度上是非结构化的。这两种二晶型MSP2(3D7和FC27)在溶液中可以等量伸展，形成淀粉样原纤维，尽管具有不同的动力学和结构特征。这些纤维具有规则的潜在β-Sheet结构，两种纤维类型都用刚果红染色，但只有FC27纤维染色硫代黄素T。3D7MSP2纤维播撒了3D7或FC27MSP2单体的纤维生长，表明MSP2的保守区参与了纤维的形成。与此一致的是，用蛋白酶K消化纤维产生了抗性多肽，其中包括MSP2的N端保守区。与重组MSP2单抗优先反应的单抗不与裂殖子表面抗原发生原位反应。感染红细胞的戊二醛交联产生的MSP2寡聚体与聚合重组MSP2形成的寡聚体相似。我们的结论是，含有类似于淀粉样蛋白纤维的分子间β-链相互作用的MSP2寡聚体可能是恶性疟原虫裂殖子表面纤维涂层的一种成分。
Several merozoite surface proteins are being assessed as potential components of a vaccine against Plasmodium falciparum, the cause of the most serious form of human malaria. One of these proteins, merozoite surface protein 2 (MSP2), is unusually hydrophilic and contains tandem sequence repeats, characteristics of intrinsically unstructured proteins. A range of physicochemical studies have confirmed that recombinant forms of MSP2 are largely unstructured. Both dimorphic types of MSP2 (3D7 and FC27) are equivalently extended in solution and form amyloid-like fibrils although with different kinetics and structural characteristics. These fibrils have a regular underlying β-sheet structure and both fibril types stain with Congo Red, but only the FC27 fibrils stain with Thioflavin T. 3D7 MSP2 fibrils seeded the growth of fibrils from 3D7 or FC27 MSP2 monomer indicating the involvement of a conserved region of MSP2 in fibril formation. Consistent with this, digestion of fibrils with proteinase K generated resistant peptides, which included the N-terminal conserved region of MSP2. A monoclonal antibody that reacted preferentially with monomeric recombinant MSP2 did not react with the antigen in situ on the merozoite surface. Glutaraldehyde cross-linking of infected erythrocytes generated MSP2 oligomers similar to those formed by polymeric recombinant MSP2. We conclude that MSP2 oligomers containing intermolecular β-strand interactions similar to those in amyloid fibrils may be a component of the fibrillar surface coat on P. falciparum merozoites.
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影响因子：
8
作者：
Bourhis, Jean-Marie;Receveur-Brechot, Veronique;Oglesbee, Michael;Zhang, Xinsheng;Buccellato, Matthew;Darbon, Herve;Canard, Bruno;Finet, Stephanie;Longhi, Sonia
通讯作者：
Longhi, Sonia
DOI：
10.1016/s0304-4165(03)00101-6
发表时间：
2003-06-20
影响因子：
3
作者：
Jayakumar, R;Kusiak, JW;Rifkind, JM
通讯作者：
Rifkind, JM
影响因子：
1.5
作者：
Angov, E;Aufiero, BM;Lyon, JA
通讯作者：
Lyon, JA
影响因子：
--
作者：
Alexander, David L.;Arastu-Kapur, Shirin;Boothroyd, John C.
通讯作者：
Boothroyd, John C.
影响因子：
4.8
作者：
Baskakov, IV;Legname, G;Cohen, FE
通讯作者：
Cohen, FE