Mucosal antibodies induced by tandem repeat of 2F5 epitope block transcytosis of HIV-1

被引:7
|
作者
Wang, Ji [1 ,2 ,3 ]
Xu, Liling [1 ,2 ,3 ]
Tong, Pei [1 ,2 ,3 ]
Chen, Ying-Hua [1 ,2 ,3 ]
机构
[1] Tsinghua Univ, Sch Life Sci, Immunol Lab, Beijing, Peoples R China
[2] Beijing Key Lab Prot Therapeut, Beijing, Peoples R China
[3] Prot Sci Lab MOE, Beijing 100084, Peoples R China
关键词
HIV-1; 2F5; epitope; Mucosal antibody; Transcytosis; HUMAN-IMMUNODEFICIENCY-VIRUS; SWINE-FEVER VIRUS; MONOCLONAL-ANTIBODIES; NEUTRALIZING ANTIBODIES; ELDKWA-EPITOPE; TYPE-1; TRANSCYTOSIS; VACCINE CANDIDATE; CRYSTAL-STRUCTURE; PROTEIN MOLECULE; EPITHELIAL-CELLS;
D O I
10.1016/j.vaccine.2011.09.032
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Induction of mucosal antibodies to prevent HIV infection is an important strategy for the HIV-1 prophylaxis. Here we report an epitope-vaccine based antigen that was able to elicit mucosal antibodies capable of blocking HIV-1 transcytosis. Because the ELDKWA epitope of neutralizing antibody 2F5 plays a crucial role in transcytosis, a series of immunogens that contain tandem copies of ELDKWA were prepared. Mice were immunized with these immunogens intranasally, and received intraperitoneal + intranasal boosters. The immunogens that contained more ELDKWA epitopes elicited higher level of mucosal ELDKWA-epitope specific IgAs and systemic IgGs. Although the antisera from the immunized mice exhibited mild neutralizing potency to HIV-1 isolates HXB2 and JRFL, the affinity purified mucosal ELDKWA-epitope specific antibodies could block the transcytosis of cell-free CNE3 (a primary isolate of subtype CRF01_AE) in human tight epithelial models. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:8542 / 8548
页数:7
相关论文
共 50 条
  • [1] The role of immunological tolerance in humoral responses to the 2F5 epitope of HIV-1
    Yang, Guang
    Holl, T.
    Nojima, Takuya
    Verkoczy, Laurent
    Moody, M.
    Haynes, Barton
    Kitamura, Daisuke
    Kelsoe, Garnett
    JOURNAL OF IMMUNOLOGY, 2013, 190
  • [2] Artificial Polyepitope HIV-1 Immunogen Containing Mimotope of 2F5 Epitope
    Shcherbakova, Nadezhda S.
    Shcherbakov, Dmitry N.
    Bakulina, Anastasiya Yu
    Karpenko, Larisa I.
    Ryzhikov, Alexander B.
    Ilyichev, Alexander A.
    PROTEIN AND PEPTIDE LETTERS, 2016, 23 (02): : 159 - 168
  • [3] The 2F5 epitope is helical in the HIV-1 entry inhibitor T-20
    Biron, Z
    Khare, S
    Quadt, SR
    Hayek, Y
    Naider, F
    Anglister, J
    BIOCHEMISTRY, 2005, 44 (41) : 13602 - 13611
  • [4] Construction of peptides mimicking a HIV-1 gp41 epitope recognized by virus-neutralizing antibodies 2F5
    Tumanova, OY
    Kuvshinov, VN
    Azaev, MS
    Masharsky, AE
    Klimov, NA
    Kozlov, AP
    Ilyichev, AA
    Sandakhchiev, LS
    MOLECULAR BIOLOGY, 2001, 35 (01) : 130 - 133
  • [5] Construction of Peptides Mimicking a HIV-1 gp41 Epitope Recognized by Virus-Neutralizing Antibodies 2F5
    O. Yu. Tumanova
    V. N. Kuvshinov
    M. Sh. Azaev
    A. E. Masharsky
    N. A. Klimov
    A. P. Kozlov
    A. A. Ilyichev
    L. S. Sandakhchiev
    Molecular Biology, 2001, 35 : 130 - 133
  • [6] Immunogenic properties of peptides mimicking a HIV-1 gp41 epitope recognized by virus-neutralizing antibodies 2F5
    Tumanova, OY
    Kuvshinov, VN
    Orlovskaya, IA
    Pronyaeva, TR
    Pokrovskii, AG
    Il'ichev, AA
    Sandakhchiev, LS
    MOLECULAR BIOLOGY, 2003, 37 (03) : 473 - 476
  • [7] Immunogenic Properties of Peptides Mimicking a HIV-1 gp41 Epitope Recognized by Virus-Neutralizing Antibodies 2F5
    O. Yu. Tumanova
    V. N. Kuvshinov
    I. A. Orlovskaya
    T. R. Pronyaeva
    A. G. Pokrovskii
    A. A. Il'ichev
    L. S. Sandakhchiev
    Molecular Biology, 2003, 37 : 473 - 476
  • [8] Membrane association and epitope recognition by HIV-1 neutralizing anti-gp41 2F5 and 4E10 antibodies
    Sanchez-Martinez, Silvia
    Lorizate, Maier
    Katinger, Hermann
    Kunert, Renate
    Nieva, Jose L.
    AIDS RESEARCH AND HUMAN RETROVIRUSES, 2006, 22 (10) : 998 - 1006
  • [9] Neutralizing antibodies induced by liposomal HIV-1 glycoprotein 41 peptide simultaneously bind to both the 2F5 or 4E10 epitope and lipid epitopes
    Matyas, Gary R.
    Wieczorek, Lindsay
    Beck, Zoltan
    Ochsenbauer-Jambor, Christina
    Kappes, John C.
    Michael, Nelson L.
    Polonis, Victoria R.
    Alving, Carl R.
    AIDS, 2009, 23 (16) : 2069 - 2077
  • [10] Structural analysis of the epitope of the anti-HIV-1 mAb 2F5 yields insights into the mechanism of neutralization and into the HIV-1 fusion process
    Pessi, Antonello
    Barbato, Gaetano
    Ingallinella, Paolo
    Hurni, William H.
    Miller, Michael D.
    Ciliberto, Gennaro
    Cortese, Riccardo
    Bazzo, Renzo
    Shiver, John W.
    Bianchi, Elisabetta
    PEPTIDE REVOLUTION: GENOMICS, PROTEOMICS & THERAPEUTICS, 2004, : 978 - 980