Abstract:
:Human immunodeficiency virus type 1 (HIV-1) transmembrane glycoprotein gp41 is targeted by broadly-reactive neutralizing antibodies 2F5 and 4E10, making it an attractive target for vaccine development. To better assess immunogenic properties of gp41, we generated five soluble glutathione S-transferase fusion proteins encompassing C-terminal 30, 64, 100, 142, or 172 (full-length) amino acids of gp41 ectodomain from M group consensus envelope sequence. Antibody responses in HIV-1-infected patients were evaluated using these proteins and overlapping peptides. We found (i) antibody responses against different regions of gp41 varied tremendously among individual patients, (ii) patients with stronger antibody responses against membrane-proximal external region exhibit broader and more potent neutralizing activity, and (iii) several patients mounted antibodies against epitopes that are near, or overlap with, those targeted by 2F5 or 4E10. These soluble gp41 fusion proteins could be an important source of antigens for future vaccine development efforts.
journal_name
Virologyjournal_title
Virologyauthors
Penn-Nicholson A,Han DP,Kim SJ,Park H,Ansari R,Montefiori DC,Cho MWdoi
10.1016/j.virol.2007.11.009subject
Has Abstractpub_date
2008-03-15 00:00:00pages
442-56issue
2eissn
0042-6822issn
1096-0341pii
S0042-6822(07)00764-7journal_volume
372pub_type
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