Beyond Viral Neutralization

AIDS Research and Human Retroviruses

Volumn 33, Issue 8, 2017, Pages 760-764

  Lewis, George K ^a   Pazgier, Marzena ^a   Evans, David T ^b,c   Ferrari, Guido ^d   Bournazos, Stylianos ^e   Parsons, Matthew S ^f   Bernard, Nicole F ^g   Finzi, Andrés ^h,i,j  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

^c UNIVERSITY OF WISCONSIN   (United States)

^d DUKE UNIVERSITY MEDICAL CENTER   (United States)

^e ROCKEFELLER UNIVERSITY   (United States)

^f UNIVERSITY OF MELBOURNE   (Australia)

^g RESEARCH INSTITUTE OF THE MCGILL UNIVERSITY HEALTH CENTRE   (Canada)

^h CENTRE HOSPITALIER DE L UNIVERSITÉ DE MONTRÉAL   (Canada)

ⁱ UNIVERSITÉ DE MONTRÉAL   (Canada)

^j MCGILL UNIVERSITY   (Canada)

more..

Author keywords

ADCC; Env; Fc; HIV 1; humanized mouse models; KIR; neutralization; NK; non neutralizing antibodies

Indexed keywords

EPITOPE; VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; NEUTRALIZING ANTIBODY;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIBODY DEPENDENT CELLULAR CYTOTOXICITY; ARTICLE; COMPLEMENT ACTIVATION; EXPERIMENTAL MODEL; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS 1 INFECTION; MOUSE; NATURAL KILLER CELL; NONHUMAN; PHAGOCYTOSIS; PRIORITY JOURNAL; VIRUS INHIBITION; VIRUS NEUTRALIZATION; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IMMUNOLOGY;

ANTIBODIES, NEUTRALIZING; ANTIBODY-DEPENDENT CELL CYTOTOXICITY; COMPLEMENT ACTIVATION; HIV ANTIBODIES; HIV INFECTIONS; HIV-1; HUMANS; PHAGOCYTOSIS;

EID: 85019210923     PISSN: 08892229     EISSN: 19318405     Source Type: Journal    
DOI: 10.1089/aid.2016.0299     Document Type: Article

References (56)

1. Ferrari G, Pollara J, Kozink D, et al.: An HIV-1 gp120 envelope human monoclonal antibody that recognizes a C1 conformational epitope mediates potent antibody-dependent cellular cytotoxicity (ADCC) activity and defines a common ADCC epitope in human HIV-1 serum. J Virol 2011;85: 7029-7036.
2. Guan Y, Pazgier M, Sajadi MM, et al.: Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding. Proc Natl Acad Sci U S A 2013;110:E69-E78.
3. Veillette M, Desormeaux A, Medjahed H, et al.: Interaction with cellular CD4 exposes HIV-1 envelope epitopes targeted by antibody-dependent cell-mediated cytotoxicity. J Virol 2014;88:2633-2644.
4. Acharya P, Tolbert WD, Gohain N, et al.: Structural definition of an antibody-dependent cellular cytotoxicity response implicated in reduced risk for HIV-1 infection. J Virol 2014;88:12895-12906.
5. Tolbert WD, Gohain N, Veillette M, et al.: Paring down HIV Env: Design and crystal structure of a stabilized inner domain of HIV-1 gp120 displaying a major ADCC target of the A32 region. Structure 2016;24:697-709.
6. Richard J, Veillette M, Brassard N, et al.: CD4 mimetics sensitize HIV-1-infected cells to ADCC. Proc Natl Acad Sci U S A. 2015;112:E2687-E2694.
7. Richard J, Pacheco B, Gohain N, et al.: Co-receptor binding site antibodies enable CD4-mimetics to expose conserved anti-cluster A ADCC epitopes on HIV-1 envelope glycoproteins. EBioMedicine. 2016;12:208-218.
8. Ding S, Verly MM, Princiotto A, et al.: Small molecule CD4-mimetics sensitize HIV-1-infected cells to ADCC by antibodies elicited by multiple envelope glycoprotein immunogens in non-human primates. AIDS Res Hum Retroviruses 2016; [Epub ahead of print]; DOI:10.1089/AID.2016.0246.
9. Ding S, Tolbert WD, Prevost J, et al.: A highly conserved gp120 inner domain residue modulates Env conformation and trimer stability. J Virol 2016;90:8395-8409.
10. Finzi A, Xiang SH, Pacheco B, et al.: Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions. Mol Cell 2010;37:656-667.
11. Sung JA, Pickeral J, Liu L, et al.: Dual-affinity re-targeting proteins direct T cell-mediated cytolysis of latently HIVinfected cells. J Clin Invest 2015;125:4077-4090.
12. Sloan DD, Lam CY, Irrinki A, et al.: Targeting HIV reservoir in infected CD4 T cells by dual-affinity re-targeting molecules (DARTs) that bind HIV envelope and recruit cytotoxic T cells. PLoS Pathog 2015;11:e1005233.
13. von Bredow B, Arias JF, Heyer LN, et al.: Comparison of antibody-dependent cell-mediated cytotoxicity and virus neutralization by HIV-1 Env-specific monoclonal antibodies. J Virol 2016;90:6127-6139.
14. Pollara J, Bonsignori M, Moody MA, Pazgier M, Haynes BF, Ferrari G: Epitope specificity of human immunodeficiency virus-1 antibody dependent cellular cytotoxicity [ADCC] responses. Curr HIV Res 2013;11:378-387.
15. Veillette M, Richard J, Pazgier M, Lewis GK, Parsons MS, Finzi A: Role of HIV-1 envelope glycoproteins conformation and accessory proteins on ADCC responses. Curr HIV Res 2016;14:9-23.
16. Lewis GK: Role of Fc-mediated antibody function in protective immunity against HIV-1. Immunology 2014;142:46-57.
17. Arias JF, Heyer LN, von Bredow B, et al.: Tetherin antagonism by Vpu protects HIV-infected cells from antibody-dependent cell-mediated cytotoxicity. Proc Natl Acad Sci U S A. 2014;111:6425-6430.
18. Alvarez RA, Hamlin RE, Monroe A, et al.: HIV-1 Vpu antagonism of tetherin inhibits antibody-dependent cellular cytotoxic responses by natural killer cells. J Virol 2014; 88:6031-6046.
19. von Bredow B, Arias JF, Heyer LN, et al.: Envelope glycoprotein internalization protects human and simian immunodeficiency virus-infected cells from antibody-dependent cell-mediated cytotoxicity. J Virol 2015;89:10648-10655.
20. Bruel T, Guivel-Benhassine F, Amraoui S, et al.: Elimination of HIV-1-infected cells by broadly neutralizing antibodies. Nat Commun 2016;7:10844.
21. Chung AW, Isitman G, Navis M, et al.: Immune escape from HIV-specific antibody-dependent cellular cytotoxicity(ADCC) pressure. Proc Natl Acad Sci U S A 2011;108:7505-7510.
22. Liu Q, Sun Y, Rihn S, et al.: Matrix metalloprotease inhibitors restore impaired NK cell-mediated antibodydependent cellular cytotoxicity in human immunodeficiency virus type 1 infection. J Virol 2009;83:8705-8712.
23. Tang CC, Isitman G, Bruneau J, et al.: Phenotypical and functional profiles of natural killer cells exhibiting matrix metalloproteinase-mediated CD16 cleavage after anti-HIV antibody-dependent activation. Clin Exp Immunol 2015; 181:275-285.
24. Grzywacz B, Kataria N, Verneris MR: CD56(dim)CD16(+) NK cells downregulate CD16 following target cell induced activation of matrix metalloproteinases. Leukemia 2007; 21:356-359.
25. Romee R, Foley B, Lenvik T, et al.: NK cell CD16 surface expression and function is regulated by a disintegrin and metalloprotease-17 (ADAM17). Blood 2013;121:3599-3608.
26. Isitman G, Lisovsky I, Tremblay-McLean A, et al.: Natural killer cell education does not affect the magnitude of granzyme B delivery to target cells by antibody-dependent cellular cytotoxicity. AIDS 2015;29:1433-1443.
27. Gooneratne SL, Center RJ, Kent SJ, Parsons MS: Functional advantage of educated KIR2DL1(+) natural killer cells for anti-HIV-1 antibody-dependent activation. Clin Exp Immunol 2016;184:101-109.
28. Parsons MS, Loh L, Gooneratne S, Center RJ, Kent SJ: Role of education and differentiation in determining the potential of natural killer cells to respond to antibodydependent stimulation. AIDS 2014;28:2781-2786.
29. Parsons MS, Wren L, Isitman G, et al.: HIV infection abrogates the functional advantage of natural killer cells educated through KIR3DL1/HLA-Bw4 interactions to mediate anti-HIV antibody-dependent cellular cytotoxicity. J Virol 2012;86:4488-4495.
30. Anfossi N, Andre P, Guia S, et al.: Human NK cell education by inhibitory receptors for MHC class I. Immunity 2006;25:331-342.
31. Charoudeh HN, Schmied L, Gonzalez A, et al.: Quantity of HLA-C surface expression and licensing of KIR2DL+ natural killer cells. Immunogenetics 2012;64:739-745.
32. Kim S, Sunwoo JB, Yang L, et al.: HLA alleles determine differences in human natural killer cell responsiveness and potency. Proc Natl Acad Sci U S A 2008;105:3053-3058.
33. Horowitz A, Djaoud Z, Nemat-Gorgani N, et al.: Class I HLA haplotypes form two schools that educate NK cells in different ways. Sci Immunol 2016;1. [Epub ahead of print]; DOI:10.1126/sciimmunol.aag1672.
34. Ward JP, Bonaparte MI, Barker E: HLA-C and HLA-E reduce antibody-dependent natural killer cell-mediated cytotoxicity of HIV-infected primary T cell blasts. AIDS 2004;18:1769-1779.
35. + T cells is directly associated with the magnitude of surface IgG binding. J Virol 2012;86:8672-8680.
36. Gooneratne SL, Richard J, Lee WS, Finzi A, Kent SJ, Parsons MS: Slaying the Trojan horse: Natural killer cells exhibit robust anti-HIV-1 antibody-dependent activation and cytolysis against allogeneic T cells. J Virol 2015;89:97-109.
37. Veillette M, Richard J, Finzi A: Uncovering HIV-1-infected cells. Oncotarget 2015;6:21791-21792.
38. Klein F, Halper-Stromberg A, Horwitz JA, et al.: HIV therapy by a combination of broadly neutralizing antibodies in humanized mice. Nature 2012;492:118-122.
39. Shingai M, Nishimura Y, Klein F, et al.: Antibodymediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia. Nature 2013;503:277-280.
40. Barouch DH, Whitney JB, Moldt B, et al.: Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys. Nature 2013; 503:224-228.
41. Caskey M, Klein F, Lorenzi JC, et al.: Viraemia suppressed in HIV-1-infected humans by broadly neutralizing antibody 3BNC117. Nature 2015;522:487-491.
42. Scheid JF, Horwitz JA, Bar-On Y, et al.: HIV-1 antibody 3BNC117 suppresses viral rebound in humans during treatment interruption. Nature 2016;535:556-560.
43. Lynch RM, Boritz E, Coates EE, et al.: Virologic effects of broadly neutralizing antibody VRC01 administration during chronic HIV-1 infection. Sci Transl Med 2015;7:319ra206.
44. Bournazos S, DiLillo DJ, Ravetch JV: The role of Fc-FcgammaR interactions in IgG-mediated microbial neutralization. J Exp Med 2015;212:1361-1369.
45. Bournazos S, Ravetch JV: Fcgamma receptor pathways during active and passive immunization. Immunol Rev 2015;268:88-103.
46. Pietzsch J, Gruell H, Bournazos S, et al.: A mouse model for HIV-1 entry. Proc Natl Acad Sci U S A 2012;109: 15859-15864.
47. Bournazos S, Klein F, Pietzsch J, Seaman MS, Nussenzweig MC, Ravetch JV: Broadly neutralizing anti-HIV-1 antibodies require Fc effector functions for in vivo activity. Cell 2014;158:1243-1253.
48. Smith P, DiLillo DJ, Bournazos S, Li F, Ravetch JV: Mouse model recapitulating human Fcgamma receptor structural and functional diversity. Proc Natl Acad Sci U S A 2012;109:6181-6186.
49. Lu CL, Murakowski DK, Bournazos S, et al.: Enhanced clearance of HIV-1-infected cells by broadly neutralizing antibodies against HIV-1 in vivo. Science 2016;352:1001-1004.
50. Bournazos S, Chow SK, Abboud N, Casadevall A, Ravetch JV: Human IgG Fc domain engineering enhances antitoxin neutralizing antibody activity. J Clin Invest 2014;124:725-729.
51. Hiatt A, Bohorova N, Bohorov O, et al.: Glycan variants of a respiratory syncytial virus antibody with enhanced effector function and in vivo efficacy. Proc Natl Acad Sci U S A 2014;111:5992-5997.
52. Sanford JE, Lupan DM, Schlageter AM, Kozel TR: Passive immunization against Cryptococcus neoformans with an isotype-switch family of monoclonal antibodies reactive with cryptococcal polysaccharide. Infect Immun 1990;58: 1919-1923.
53. Schlageter AM, Kozel TR: Opsonization of Cryptococcus neoformans by a family of isotype-switch variant antibodies specific for the capsular polysaccharide. Infect Immun 1990;58:1914-1918.
54. Varshney AK, Wang X, Aguilar JL, Scharff MD, Fries BC: Isotype switching increases efficacy of antibody protection against staphylococcal enterotoxin B-induced lethal shock and Staphylococcus aureus sepsis in mice. MBio 2014; 5:e01007-e01014.
55. DiLillo DJ, Tan GS, Palese P, Ravetch JV: Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo. Nat Med 2014;20:143-151.
56. DiLillo DJ, Palese P, Wilson PC, Ravetch JV: Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection. J Clin Invest 2016;126: 605-610.