Mitochondrial H+-ATPase is an enzyme complex, which is located in the mitochondrial inner membrane and plays a crucial role in coupling phosphorylation. It exhibits a dualfunction in catalyzing ATP synthesis and hydro...Mitochondrial H+-ATPase is an enzyme complex, which is located in the mitochondrial inner membrane and plays a crucial role in coupling phosphorylation. It exhibits a dualfunction in catalyzing ATP synthesis and hydrolyzing ATP. The H+-ATPase complex is known to consist of three parts, i. e. F1, the hydrophobic protein （F0） and OSGP. F1 is a water-soluble protein which is in contact with the aqueous medium, bearing the展开更多
The Human immunodeficiency virus type 1(HIV-1) gp41 membrane proximal external region(MPER) is targeted by broadly neutralizing antibodies(e.g. 2F5, 4E10, Z13 e and m66.6), which makes this region a promising target f...The Human immunodeficiency virus type 1(HIV-1) gp41 membrane proximal external region(MPER) is targeted by broadly neutralizing antibodies(e.g. 2F5, 4E10, Z13 e and m66.6), which makes this region a promising target for vaccine design. One strategy to elicit neutralizing antibodies against the MPER epitope is to design peptide immunogens mimicking neutralization structures. To probe 2F5-like neutralizing antibodies, two yeast-displayed antibody libraries from peripheral blood mononuclear cells from a HIV-1 patient were screened against the 2F5 epitope peptide SP62. Two 2F5-like antibodies were identified that specifically recognized SP62. However,these antibodies only weakly neutralized HIV-1 primary isolates. The epitopes recognized by these two 2F5-like antibodies include not only the 2F5 epitope(amino acids(aa) 662–667 in the MPER)but also several other residues(aa 652–655) locating at the N-terminus in SP62. Experimental results suggest that residues of SP62 adjacent to the 2F5 epitope influence the response of broadly neutralizing 2F5-like antibodies in vaccination. Our findings may aid the design of vaccine immunogens and development of therapeutics against HIV-1 infection.展开更多
文摘Mitochondrial H+-ATPase is an enzyme complex, which is located in the mitochondrial inner membrane and plays a crucial role in coupling phosphorylation. It exhibits a dualfunction in catalyzing ATP synthesis and hydrolyzing ATP. The H+-ATPase complex is known to consist of three parts, i. e. F1, the hydrophobic protein （F0） and OSGP. F1 is a water-soluble protein which is in contact with the aqueous medium, bearing the
基金supported by the Natural Science Foundation of Guangdong (No. 2015A030313741)the National Natural Science Foundation of China (No. 31440041)+2 种基金Shenzhen Peacock Innovation Plan Fund (No. KQCX20140520154115029)Shenzhen Knowledge Innovation Program (No. JCYJ20140901003939 026)Novo Nordisk A/S-Chinese Academy of Sciences Research Fund (No. NNCAS-2013-9)
文摘The Human immunodeficiency virus type 1(HIV-1) gp41 membrane proximal external region(MPER) is targeted by broadly neutralizing antibodies(e.g. 2F5, 4E10, Z13 e and m66.6), which makes this region a promising target for vaccine design. One strategy to elicit neutralizing antibodies against the MPER epitope is to design peptide immunogens mimicking neutralization structures. To probe 2F5-like neutralizing antibodies, two yeast-displayed antibody libraries from peripheral blood mononuclear cells from a HIV-1 patient were screened against the 2F5 epitope peptide SP62. Two 2F5-like antibodies were identified that specifically recognized SP62. However,these antibodies only weakly neutralized HIV-1 primary isolates. The epitopes recognized by these two 2F5-like antibodies include not only the 2F5 epitope(amino acids(aa) 662–667 in the MPER)but also several other residues(aa 652–655) locating at the N-terminus in SP62. Experimental results suggest that residues of SP62 adjacent to the 2F5 epitope influence the response of broadly neutralizing 2F5-like antibodies in vaccination. Our findings may aid the design of vaccine immunogens and development of therapeutics against HIV-1 infection.
