Xueling Wu, MD, PhD

  • Associate Professor of Medical Sciences (in Medicine)
Profile Headshot


Academic Appointments

  • Associate Professor of Medical Sciences (in Medicine)


  • Chinese


  • Female

Credentials & Experience

Education & Training

  • MD, 1994 Medicine, Tongji Medical University (China)
  • PhD, 2002 Microbiology, Univ of Alabama/Birmingham Hospital
  • Fellowship: 2006 Fred Hutchinson Cancer Research Center

Honors & Awards

  • 2003-2006: Postdoctoral Fellowship, Cancer Research Institute, New York
  • 2005: Keystone Symposia Scholarship, NIAID
  • 2006: Keystone Symposia Conference Assistance, NIAID
  • 2010: Oral Presentation, AIDS Vaccine 2010 Conference, Atlanta, GA
  • 2010-2012: Director’s Award, Vaccine Research Center, NIAID
  • 2010-2012: Employee Merit Award, NIAID
  • 2012: Invited Speaker, University of Montreal, Montreal, Canada
  • 2013: Invited Speaker, Icahn School of Medicine at Mount Sinai, New York, NY
  • 2013: Invited Speaker, Nanfang Hospital, Southern Medical University, Guangzhou, China
  • 2014: Oral Presentation and Panel Moderator, CROI, Boston, MA
  • 2015: Invited Speaker, the 4th Medical Forum for Chinese Scientists, Shanghai 10th People’s Hospital, Shanghai, China
  • 2016: Invited Speaker, Boston Medical Center, Boston University, Boston, MA


The overall research interest of Wu Lab is to study human B cell responses to viral infections by discovering and characterizing potent broadly neutralizing antibodies (bNAbs). The Wu lab has ongoing research in three areas:

  1. HIV
  2. Viruses with pandemic threats such as Influenza, Coronaviruses, and Ebolaviruses
  3. Autoantibodies

HIV broadly neutralizing antibodies (bNAbs)

While at the Vaccine Research Center (VRC), NIAID, NIH, Dr. Wu contributed to the discovery of an important class of HIV bNAbs, VRC01 and its class that target the CD4-binding site of the viral envelope (Env) glycoprotein. VRC01 was later tested in the first “antibody mediated prevention” (AMP) human trial and demonstrated 75% efficacy of blocking VRC01-sensitive viral strains. The Wu Lab continues to optimize and apply advanced techniques such as 10X Genomics Immune Profiling to efficiently identify HIV bNAbs and mAbs that mediate antibody-dependent cellular cytotoxicity (ADCC) and antibody-dependent cellular phagocytosis (ADCP).

Based on our surprise finding of two HIV bNAb lineages that class-switched to both IgG and IgA, published in Jia et alCell Host & Microbe 2020, 27: 963, we have for the first time identified bona fide HIV IgA bNAbs. Because HIV spreads mainly through mucosal exposures, the dominant IgA at mucosa compartments has long been the class of antibodies desired at the portal of entry to block infection. We have thus focused our bNAb efforts to IgA and aim to test whether IgA, in its mucosal form – secretory IgA (SIgA), is better than IgG at blocking infection in a SHIV macaque challenge model. Our research project aims to address the following questions:

  • Compared to IgG, what is the frequency of IgA bNAb response to HIV infection?
  • Compared to IgG, what are the epitopes that IgA bNAbs target on HIV Env?
  • Compared to IgG, what are the sequence signatures of IgA bNAbs?
  • Compared to IgG, would IgA, in its mucosal form SIgA, enhance its HIV neutralization potency in vitro?
  • Compared to IgG, would IgA, in its mucosal form SIgA, better at blocking SHIV infection in a macaque challenge model?

Answers to these questions would help study design for more mucosal targeted antibody-mediated protections from HIV.

To facilitate HIV bNAb clinical trials, an accurate and sensitive bNAb susceptibility assay with a quick turnaround time is needed. The Wu Lab is actively working with other labs at ADARC/CUMC to develop an integrated approach with two prongs: a phenotypic (Env function) assay for bulk Env neutralization assessment with Env-barcoding and a genotypic (Env sequence) algorithm for high-throughput Env nanopore sequencing and prediction of bNAb susceptibility.

HIV env evolution and bNAb lineages

To understand how HIV bNAbs are developed and driven by HIV env gene evolution, the Wu Lab has longitudinally tracked env evolution and bNAb development in SHIV-infected rhesus macaques and HIV-infected humans. In Jia et alJ Virol 2016, 90: 4017, we reported 5 SHIVSF162P3N-infected rhesus macaques and 9 HIV-infected humans who developed bNAbs. Of the 5 macaques, we performed longitudinal plasma neutralization and defined sequential development of NAbs in these animals. From three macaques, GB40, FF69, and FD83, we isolated sequential Env sequences and identified in each animal 3-5 sequential NAb waves from the initial narrow autologous to later broad responses. To gain insights to the NAb targets, we examined specific amino acid changes in Env over time and found that gp120 V5 was targeted by the 1st wave of NAbs, as reported in Jia et alViruses 2018, 10: 262. These findings led to our working model that over the course of viral infection, the initial autologous NAbs gradually broaden to gain neutralization breadth; under this model, we tested two possible mechanisms – “epitope drifting” and “epitope optimization” for NAb broadening in these animals. Our follow-up studies support the mechanism of “epitope optimization” for bNAb development. Of the 9 HIV-infected humans who developed bNAbs, we obtained longitudinal blood samples from 7 subjects and determined their bNAb dynamics. Like the SHIV-macaque study above, we are currently isolating sequential Envs from these human subjects to map Env targets for bNAbs and test if the mechanism of “epitope optimization” holds for bNAb development in these human subjects.

Derived from this project, a powerful tool that the Wu Lab has advanced is the B cell receptor (BCR) repertoire sequencing. We published the workflow of an unbiased 5’ RACE (rapid amplification of cDNA ends) PCR and Illumina MiSeq of BCR repertoires in Waltari et alFrontiers in Immunology 2018, 9: 628. We generated the BCR repertoire sequence data from two SHIV-infected rhesus macaques. During the initial analysis of macaque BCR repertoires, we realized that the current macaque IGHV germline database is incomplete and thus obtained the IGHV germlines of 4 macaques included in our study. Our analyses revealed new macaque IGHV germline genes, thus contributing to the non-human primate IGHV germline gene collection and database. With the IGHV germlines determined for each macaque, we are applying the animal’s self-germline reference to analyze expressed BCR repertoires and antibody lineages.

HIV vaccine research

While at the Fred Hutchinson Cancer Research Center, Dr. Wu isolated a panel of mother-to-child transmitted Envs including BG505, which was later used for the first successful construction of soluble Env trimer protein (SOSIP) and extensively tested as an Env immunogen that closely resembles the HIV native Env trimer. Our isolated HIV bNAb M4008_N1 binds to a novel V3 crown epitope revealed in Chan et alNature Communications, 2021, 12: 6464, which provided the foundation for a V3-based Env immunogen study led by Dr. X-P Kong at NYU School of Medicine. The Wu Lab has been actively involved in and instrumental to Dr. Kong’s HIV vaccine programs, which recently yielded exciting results implicating a major breakthrough. The Wu Lab will remain committed to Dr. Kong’s efforts to develop a successful HIV vaccine.

Viruses with pandemic threats:

Since the global breakout of COVID-19 in 2020, NAbs and vaccines have been quickly identified and developed for treatment and prevention. However, viral escape from vaccines and NAbs has been a common theme for COVID-19. The next challenge and research interest for COVID-19 is to develop pan-coronavirus vaccines and identify truly broad and potent bNAbs, which may exist in a subset of convalescent cases and vaccinees. Working with Dr. Andres Finzi at University of Montreal, the Wu Lab has designed a probing strategy to identify broadly reactive B cells from a Canadian study cohort, and this work is currently ongoing. Since COVID-19 primarily targets the airway – a mucosal compartment, the Wu Lab is also investigating its IgA response, with an ongoing collaboration with Dr. Rebecca Powell at Mount Sinai to isolate mAbs from breastmilk of COVID-19 convalescent cases and vaccinees.

For Influenza, the Wu Lab has isolated four mAbs directed to the hemagglutinin (HA) from a 2013 H7N9 convalescent case in Hong Kong. Two HA1-directed mAbs neutralized H7N9 and protected mice from a lethal challenge. Cryo-EM structures revealed that these mAbs bind to a β14-centered surface partially overlapping with the antigenic site D of HA1 and disrupt the 220-loop that makes hydrophobic contacts with sialic acid on the adjacent protomer, thus affectively blocking viral entry. Both mAbs remained active to later H7N9 isolates from 2016-2017. The HA2-directed mAb lacked neutralizing activity but protected mice from lethal challenge when engineered to mouse IgG2a with Fc effector function. Used in combination with a suboptimal dose HA1-directed neutralizing mAb, the HA2-directed mAb augmented mouse protection. The Columbia University Tech Office has filed a provisional application to patent these mAbs. As Influenza is well known for its genetic reassortment and antigenic drift and shift, the next challenge and research interest for Influenza is also developing universal vaccines and finding truly broad and potent bNAbs, which is an interest of research in the Wu Lab. Since Influenza primarily targets the airway, the Wu Lab is also interested in its IgA response.

For Ebolaviruses, the current two in-use vaccines, rVSV-ZEBOV and a two-dose combination of Ad26.ZEBOV and MVA-BN-Filo, have yet to demonstrate protection against multiple Ebolavirus species. Our collaborators at the Southern Medical University in China immunized (I.M.) 6 Chinese rhesus macaques with Zaire, Sudan, and Bundibugyo glycoproteins (GPs) in DNA and protein to elicit bNAb responses. All immunized macaques mounted high plasma anti-GP and anti-Ebola neutralizing titers, demonstrating the feasibility for GP-based vaccines to elicit bNAbs that cover all three major Ebola species, Zaire, Sudan, and Bundibugyo. The top three macaques that developed the most robust cross-reactive NAbs can be used for bNAb isolation. However, mAbs have not been derived from these animals because the techniques for mAb isolation are not available on site at the Southern Medical University in China. With additional funding, the Wu Lab aims to ship these macaque specimens to ADARC/CUMC to isolate anti-Ebola bNAbs.



Recently during the COVID-19 pandemic, the Wu Lab has worked with Dr. Wei Jiang at Medical University of South Carolina to examine antibody responses following COVID-19 infection and mRNA vaccination. Based on our findings of elevated anti-IFN-α autoantibodies both in COVID-19 infection and mRNA vaccination cases, we proposed to further probe these autoantibodies for mechanisms of production, affinity maturation, antigen recognition, and immune regulatory functions. To isolate anti-IFN-α autoantibodies, the Wu Lab has developed a B cell probing strategy, i.e., using IFN-β, which has a relatively higher binding affinity to IFN α/β receptor (IFNAR) than IFN-α to block IFNAR on B cells, prior to staining BCRs with an IFN-α antigen. We have tested the staining and sorting strategy using PBMCs from a donor who presented heightened levels of plasma neutralizing anti-IFN-α autoantibodies. The sorted IFN-α+ B cells have been processed for 10X Genomics. We are in the process of characterizing mAbs from these sorted B cells and testing their functions to neutralize IFN-α-mediated activity. Although in acute viral infections such as COVID-19, anti-IFN-α autoantibodies are thought to dampen IFN-α-mediated antiviral activity thus fueling disease severity, these mAbs may be beneficial in treating inflammatory diseases and chronic viral infections where IFN-α plays a role in pathogenesis.

Dr. Wei Jiang also has a longstanding expertise in anti-CD4 autoantibodies in HIV-infected individuals. Up to 25% of people with HIV on antiretroviral therapy (ART) fail to restore peripheral CD4+ T cells to the levels of healthy controls. Dr. Jiang determined that anti-CD4 IgGs from non-responders (CD4+ T cell counts < 350 cells/μL) mediate CD4+ T cell death via ADCC and contribute to poor CD4+ T cell recovery from suppressive ART. The pathogenic ADCC anti-CD4 IgGs are even more profound in HIV-infected cocaine users than non-users. We have proposed to isolate anti-CD4 autoantibodies presenting ADCC activity, particularly in HIV-infected cocaine users, to further investigate the mechanisms of autoantibody production, affinity maturation, antigen recognition, and immune regulatory functions.

With well-established mAb expertise and techniques, the Wu Lab hopes to build an antibody-based biobankto zoonotic viruses with pandemic potential to prepare for future pandemics. After COVID-19, preparedness for future pandemics is an area of research with high enthusiasm. The viruses of interest may include additional coronaviruses such as bat RsSHC014-CoV, porcine epidemic diarrhea virus (PEDV), porcine deltacoronavirus (PDCoV), and swine acute diarrhea syndrome coronavirus (SADS-CoV), Influenza such as H1N1 G4 EA, as well as Marburg, Nipah, and Lassa viruses. We propose to immunize human antibody V-gene knock-in micethat are being developed by Genomab to affinity mature NAbs against the proposed zoonotic viruses, to which there is no or limited human antibody data available. Alternatively, Dr. Moriya Tsuji at ADARC/CUMC has developed human immune system (HIS) CD4+ T and B cell (CD4/B) mice that can be used for immunizations. Analysis of antiviral NAbs ahead of time offers critical knowledge of vulnerabilities on viral surface proteins that mediate viral entry, which is crucial to inform viral targets for vaccine development. The impact of this project, if successful, will be huge to provide potent NAbs as a quick response to future pandemics. With additional funding, the Wu Lab will be able to execute this idea of research.  


Selected Publications

  • Wu X and Jackson S. Plasma and salivary IgG subclasses in HIV-1 infection: evidence for both local synthesis and transudation of IgG in parotid saliva. AIDS Research and Human Retroviruses 2000, 16: 1423-1431
  • Wu X and Jackson S. Plasma and salivary IgA subclasses and IgM in HIV-1-infected individuals.
  • Wu X and Jackson S. A longitudinal study of plasma and salivary antibodies in HIV-1 infection. Viral Immunology 2002, 15: 323-333
  • Wu X, Hall S and Jackson S. Tropism-restricted neutralization by secretory IgA from parotid saliva of HIV-1-infected individuals. AIDS Research and Human Retroviruses 2003, 19: 275-281
  • Moore J*, Wu X*, Kulhavy R, Tomana M, Novak J, Moldoveanu Z, Brown R, Goepfert P and Mestecky J. Increased levels of galactose-deficient IgG in sera of HIV-1-infected individuals. AIDS 2005, 19: 381-389 *equal contribution
  • Wu X, Parast A, Richardson B, Nduati R, John-Stewart G, Mbori-Ngacha D, Rainwater S and Overbaugh J. Neutralization escape variants of HIV-1 are transmitted from mother to infant. Journal of Virology 2006, 80: 835-844 Spotlight paper
  • Sagar M, Wu X, Lee S and Overbaugh J. HIV-1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. Journal of Virology 2006, 80: 9586-9598
  • Rainwater S, Wu X, Nduati R, Nedellec R, Mosier D, John-Stewart G, Mbori-Ngacha D and Overbaugh J. Cloning and characterization of functional subtype A HIV-1 envelope variants transmitted through breastfeeding. Current HIV Research 2007, 5: 189-197
  • Li Y, Migueles S, Welcher B, Svehla K, Phogat A, Louder M, Wu X, Shaw G, Connors M, Wyatt R and Mascola J. Broad HIV-1 neutralization mediated by CD4-binding site antibodies. Nature Medicine 2007, 13: 1032-1034
  • Williams D, Piantadosi A, Wu X, Forthal D, Landucci G, Pineda M, Kimata J and Overbaugh J. Heavily glycosylated, highly fit SIVMne variants continue to diversify and undergo selection after transmission to a new host and they elicit early antibody dependent cellular responses but delayed neutralizing antibody responses. Virology Journal 2008, 5: 90
  • Wu X, Sambor A, Nason M, Yang Z, Wu L, Zolla-Pazner S, Nabel G and Mascola J. Soluble CD4 broadens neutralization of V3-directed monoclonal antibodies and guinea pig vaccine sera against HIV-1 subtype B and C reference viruses. Virology 2008, 380: 285-295
  • Li Y, Svehla K, Louder M, Wycuff D, Phogat S, Tang M, Migueles S, Wu X, Phogat A, Shaw G, Connors M, Hoxie J, Mascola J and Wyatt R. Analysis of neutralization specificities in polyclonal sera derived from human immunodeficiency virus type 1-infected individuals. Journal of Virology 2009, 83: 1045-1059
  • Provine N, Puryear W, Wu X, Overbaugh J and Haigwood N. The infectious molecular clone and pseudotyped virus models of human immunodeficiency virus type 1 exhibit significant differences in virion composition with only moderate differences in infectivity and inhibition sensitivity. Journal of Virology 2009, 83: 9002-9007
  • Wu X*, Zhou T*, O’Dell S, Wyatt R, Kwong P and Mascola J. Mechanism of HIV-1 resistance to monoclonal antibody b12 that effectively targets the site of CD4 attachment. Journal of Virology 2009, 83: 10892-10907 spotlight paper
  • Chen L*, Kwon Y*, Zhou T*, Wu X, O’Dell S, Cavacini L, Hessell A, Pancera M, Tang M, Xu L, Yang Z, Zhang M, Arthos J, Burton D, Dimitrov D, Nabel G, Posner M, Sodroski J, Wyatt R, Mascola J and Kwong P. Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 2009, 326: 1123-1127 *equal contribution
  • Pancera M, McLellan J*, Wu X*, Zhu J*, Changela A, Schmidt S, Yang Y, Zhou T, Phogat S, Mascola J and Kwong P. Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1. Journal of Virology 2010, 84: 8098-8110 spotlight paper
  • Wu X*, Yang Z*, Li Y*, Hogerkorp C, Schief W, Seaman M, Zhou T, Schmidt S, Wu L, Xu L, O’Dell S, McKee K, Longo N, Louder M, Wycuff D, Feng Y, Guenaga J, Doria-Rose N, Connors M, Kwong P, Roederer M, Wyatt R, Nabel G* and Mascola J*. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 2010, 329: 856-861
  • Zhou T, Georgiev I*, Wu X*, Yang Z*, Dai K, Finzi A, Kwon Y, Scheid J, Shi W, Xu L, Yang Y, Zhu J, Nussenzweig M, Sodroski J, Shapiro L, Nabel G, Mascola J and Kwong P. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010, 329: 811-817
  • Changela A, Wu X*, Yang Y*, Zhang B*, Zhu J*, Nardone G, O’Dell S, Pancera M, Gorny M, Phogat S, Robinson J, Stamatatos L, Zolla-Pazner S, Mascola J and Kwong P. Crystal structure of human antibody 2909 reveals conserved features of quaternary structure-specific antibodies that potently neutralize HIV-1. Journal of Virology 2011, 85: 2524-2535
  • Wu X, Changela A, O’Dell S, Schmidt S, Pancera M, Yang Y, Zhang B, Gorny M, Phogat S, Robinson J, Stamatatos L, Zolla-Pazner S, Kwong P and Mascola J. Immunotypes of a quaternary site of HIV-1 vulnerability and their recognition by antibodies. Journal of Virology 2011, 85: 4578-4585
  • Li Y, O'Dell S, Walker L, Wu X, Guenaga J, Feng Y, Schmidt S, McKee K, Louder M, Ledgerwood J, Graham B, Haynes B, Burton D, Wyatt R and Mascola J. Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01. Journal of Virology 2011, 85: 8954-8967
  • Wu X*, Zhou T*, Zhu J*, Zhang B, Georgiev I, Wang C, Chen X, Longo N, Louder M, McKee K, O’Dell S, Perfetto S, Schmidt S, Shi W, Wu L, Yang Y, Yang Z, Yang Z, Zhang Z, Bonsignori M, Crump J, Kapiga S, Sam N, Haynes B, Simek M, Burton D, Koff W, Doria-Rose N, Connors M, NISC Comparative Sequencing Program, Mullikin J, Nabel G, Roederer M, Shapiro L, Kwong P* and Mascola J*. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 2011, 333: 1593-1602 cover
  • Bonsignori M, Montefiori D, Wu X, Chen X, Hwang K, Tsao C, Kozink D, Parks R, Tomaras G, Crump J, Kapiga S, Sam N, Kwong P, Kepler T, Liao H, Mascola J and Haynes B. Two distinct broadly neutralizing antibody specificities of different clonal lineages in a single HIV-1- infected donor: implications for vaccine design. Journal of Virology 2012, 86: 4688-4692
  • Falkowska E, Ramos A, Feng Y, Zhou T, Moquin S, Walker L, Wu X, Seaman M, Wrin T, Kwong P, Wyatt R, Mascola J, Poignard P and Burton D. PGV04, an HIV-1 gp120 CD4 binding site antibody, is broad and potent in neutralization but does not induce conformational changes characteristic of CD4. Journal of Virology 2012, 86: 4394-4403
  • Kwon Y, Finzi A, Wu X, Dogo-Isonagie C, Lee L, Moore L, Schmidt S, Stuckey J, Yang Y, Zhou T, Zhu J, Vicic D, Debnath A, Shapiro L, Bewley C, Mascola J, Sodroski J and Kwong P. Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops. PNAS 2012, 109: 5663-5668
  • Wu X, Wang C, O'Dell S, Li Y, Keele B, Yang Z, Imamichi H, Doria-Rose N, Hoxie J, Connors M, Shaw G, Wyatt R and Mascola J. Selection pressure on HIV-1 envelope by broadly neutralizing antibodies to the conserved CD4-binding site. Journal of Virology 2012, 86: 5844-5856
  • Li Y, O'Dell S, Wilson R, Wu X, Schmidt S, Hogerkorp C, Louder M, Longo N, Poulsen C, Guenaga J, Chakrabarti B, Doria-Rose N, Roederer M, Connors M, Mascola J and Wyatt R. HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully-cleaved envelope glycoproteins. Journal of Virology 2012, 86: 11231-11241
  • Zhu J, O'Dell S, Ofek G, Pancera M, Wu X, Zhang B, Zhang Z, NISC Comparative Sequencing Program, Mullikin J, Simek M, Burton D, Koff W, Shapiro L, Mascola J and Kwong P. Somatic populations of PGT135-137 HIV-1-neutralizing antibodies identified by 454 pyrosequencing and bioinformatics. Frontiers in Microbiology 2012, 3: 315
  • Ota T, Doyle-Cooper C, Cooper A, Huber M, Falkowska E, Doores K, Hangartner L, Le K, Sok D, Jardine J, Lifson J, Wu X, Mascola J, Poignard P, Binley J, Chakrabarti B, Schief W, Wyatt R, Burton D and Nemazee D. Anti-HIV B cell lines as candidate vaccine biosensors. Journal of Immunology 2012, 189: 4816-4824
  • Joyce G, Kanekiyo M, Xu L, Biertümpfel C, Boyington J, Moquin S, Shi W, Wu X, Yang Z, Yang Y, Zhang B, Zheng A, Zhou T, Zhu J, Mascola J, Kwong P and Nabel G. Outer domain of HIV-1 gp120: antigenic optimization, structural malleability, and crystal structure with antibody VRC-PG04. Journal of Virology 2013, 87: 2294-2306
  • Zhou T*, Zhu J*, Wu X, Moquin S, Zhang B, Acharya P, Georgiev I, Altae-Tran H, Chuang G, Joyce G, Kwon Y, Longo N, Louder M, Luongo T, McKee K, Schramm C, Skinner J, Yang Y, Yang Z, Zhang Z, Zheng A, Bonsignori M, Haynes B, Scheid J, Nussenzweig M, Simek M, Burton D, Koff W, NISC Comparative Sequencing Program, Mullikin J, Connors M, Shapiro L, Nabel G, Mascola J and Kwong P. Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity 2013, 39: 245-258
  • Zhu J, Wu X, Zhang B, McKee K, O'Dell S, Soto C, Zhou T, Casazza J, NISC Comparative Sequencing Program, Mullikin J, Kwong P, Mascola J and Shapiro L. De novo identification of VRC01-class HIV-1-neutralizing antibodies by next-generation sequencing of B cell transcripts. PNAS 2013, 110: E4088-4097
  • Kepler T, Liao H, Alam S, Bhaskarabhatla R, Zhang R, Yandava C, Stewart S, Anasti K, Kelsoe G, Parks R, Lloyd K, Stolarchuk C, Pritchett J, Solomon E, Friberg E, Morris L, Karim S, Cohen M, Walter E, Moody M, Wu X, Altae-Tran H, Georgiev I, Kwong P, Boyd S, Fire A, Mascola J and Haynes B. Immunoglobulin gene insertions and deletions in the affinity maturation of HIV-1 broadly reactive neutralizing antibodies. Cell Host & Microbe 2014, 16: 304-313
  • Rudicell R, Kwon Y, Ko S, Pegu A, Louder M, Georgiev I, Wu X, Zhu J, Boyington J, Chen X, Shi W, Yang Z, Doria-Rose N, McKee K, O'Dell S, Schmidt S, Chuang G, Druz A, Soto C, Yang Y, Zhang B, Zhou T, Todd J, Lloyd K, Eudailey J, Roberts K, Donald B, Bailer R, Ledgerwood J, NISC Comparative Sequencing Program, Mullikin J, Shapiro L, Koup R, Graham B, Nason M, Connors M, Haynes B, Rao S, Roederer M, Kwong P, Mascola J and Nabel G. Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo. Journal of Virology 2014, 88: 12669-12682
  • Lynch R, Wong P, Tran L, O’Dell S, Nason M, Li Y, Wu X and Mascola J. HIV-1 fitness cost associated with escape from the VRC01 class of CD4 binding site neutralizing antibodies. Journal of Virology 2015, 89: 4201-4213
  • Wu X*, Zhang Z*, Schramm C*, Joyce G*, Kwon Y*, Zhou T*, Sheng Z*, Zhang B, O’Dell S, McKee K, Georgiev I, Chuang G, Longo N, Saunders K, Soto C, Srivatsan S, Yang Y, Bailer R, Louder M, NISC Comparative Sequencing Program, Mullikin J, Connors M, Kwong P*, Mascola J* and Shapiro L*. Maturation and diversity of the VRC01-antibody lineage over 15 years of chronic HIV-1 infection. Cell 2015, 161: 470-485
  • Zhou T*, Lynch R*, Chen L*, Acharya P*, Wu X, Doria-Rose N, Joyce M, Lingwood D, Soto C, Bailer R, Ernandes M, Kong R, Longo N, Louder M, McKee K, O’Dell S, Schmidt S, Tran L, Yang Z, Druz A, Luongo T, Moquin S, Srivatsan S, Yang Y, Zhang B, Zheng A, Pancera M, Kirys T, Georgiev I, Gindin T, Peng H, Yang A, NISC Comparative Sequencing Program, Mullikin J, Gray M, Stamatatos L, Burton D, Koff W, Cohen M, Haynes B, Casazza J, Connors M, Corti D, Lanzavecchia A, Sattentau Q, Weiss R, West A Jr., Bjorkman P, Scheid J, Nussenzweig M, Shapiro L, Mascola J* and Kwong P*. Structural repertoire of HIV-1-neutralizing antibodies targeting the CD4 supersite in 14 donors. Cell 2015, 161: 1280-1292.
  • Gorman J, Soto C, Yang M, Davenport T, Guttman M, Bailer R, Chambers M, Chuang G-Y, DeKosky B, Doria-Rose N, Druz A, Ernandes M, Georgiev I, Jarosinski M, Joyce M, Lemmin T, Leung S, Louder M, McDaniel J, Narpala S, Pancera M, Stuckey J, Wu X, Yang Y, Zhang B, Zhou T, NISC Comparative Sequencing Program, Mullikin J, Baxa U, Georgiou G, McDermott A, Bonsignori M, Haynes B, Moore P, Morris L, Lee K, Shapiro L, Mascola J, Kwong P. Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design. Nature Structural & Molecular Biology 2016, 23: 81
  • Jia M, Lu H, Markowitz M, Cheng-Mayer C and Wu X. Development of broadly neutralizing antibodies and their mapping by monomeric gp120 in HIV-1 infected humans and SHIVSF162P3N infected macaques. Journal of Virology 2016, 90: 4017-4031
  • Wu X and Kong XP. Antigenic landscape of the HIV-1 envelope and new immunological concepts defined by HIV-1 broadly neutralizing antibodies. Current Opinion in Immunology 2016, 42: 56-64 Review
  • Lin N, Gonzalez OA, Registre L, Becerril C, Etemad B, Lu H, Wu X, Lockman S, Essex M, Moyo S, Kuritzkes DR and Sagar M. Humoral immune pressure selects for HIV-1 CXC-chemokine receptor 4-using variants. EBioMedicine 2016, 8: 237-247
  • Joyce M, Wheatley A, Thomas P, Chuang G-Y, Soto C, Bailer R, Druz A, Georgiev I, Gillespie R, Kanekiyo M, Kong W, Leung K, Narpala S, Prabhakaran M, Yang E, Zhang B, Zhang Y, Asokan M, Boyington J, Bylund T, Darko S, Lees C, Ransier A, Shen C-H, Wang L, Whittle J, Wu X, Yassine H, Santos C, Matsuoka Y, Tsybovsky Y, Baxa U, NISC Comparative Sequencing Program, Mullikin J, Subbarao K, Douek D, Graham B, Koup R, Ledgerwood J, Roederer M, Shapiro L, Kwong P, Mascola J, McDermott A. Vaccine-induced antibodies that neutralize Group 1 and Group 2 Influenza A viruses. Cell 2016, 166: 609
  • Richard J, Pacheco B, Gohain N, Veillette M, Ding S, Alsahafi N, Tolbert WD, Prévost J, Chapleau JP, Coutu M, Jia M, Brassard N, Park J, Courter JR, Melillo B, Martin L, Tremblay C, Hahn BH, Kaufmann DE, Wu X, Smith AB 3rd, Sodroski J, Pazgier M and Finzi A. 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
  • Jiang X, Totrov M, Li W, Sampson J, Williams C, Lu H, Wu X, Lu S, Wang S, Zolla-Pazner S and Kong X-P. Rationally designed immunogens targeting HIV-1 gp120 V1V2 induce distinct conformation-specific antibody responses in rabbits. Journal of Virology 2016, 90: 11007− 11019 
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