R C Gallo

University of Maryland, Baltimore, Baltimore, Maryland, United States

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Publications (983)11622.22 Total impact

  • Anthony L. DeVico · George K. Lewis · Robert C. Gallo ·

    Philosophical Transactions of The Royal Society B Biological Sciences 11/2015; 370(1681):20150199. DOI:10.1098/rstb.2015.0199 · 7.06 Impact Factor
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    ABSTRACT: Although in decline after successful anti-HIV therapy, B-cell lymphomas are still elevated in HIV-1-seropositive (HIV+) persons, and the mechanisms are obscure. The HIV-1 matrix protein p17 persists in germinal centers long after HIV-1 drug suppression, and some p17 variants (vp17s) activate Akt signaling and promote growth of transformed B cells. Here we show that vp17s derived from four of five non-Hodgkin lymphoma (NHL) tissues from HIV+ subjects display potent B-cell growth-promoting activity. They are characterized by amino acid insertions at position 117-118 (Ala-Ala) or 125-126 (Gly-Asn or Gly-Gln-Ala-Asn-Gln-Asn) among some other mutations throughout the sequence. Identical dominant vp17s are found in both tumor and plasma. Three of seven plasma samples from an independent set of NHL cases manifested multiple Ala insertions at position 117-118, and one with the Ala-Ala profile also promoted B-cell growth and activated Akt signaling. Ultradeep pyrosequencing showed that vp17s with C-terminal insertions are more frequently detected in plasma of HIV+ subjects with than without NHL. Insertion of Ala-Ala at position 117-118 into reference p17 (refp17) was sufficient to confer B-cell growth-promoting activity. In contrast, refp17 bearing the Gly-Asn insertion at position 125-126 did not, suggesting that mutations not restricted to the C terminus can also account for this activity. Biophysical analysis revealed that the Ala-Ala insertion mutant is destabilized compared with refp17, whereas the Gly-Asn form is stabilized. This finding provides an avenue for further exploration of structure function relationships and new treatment strategies in combating HIV-1-related NHL.
    Proceedings of the National Academy of Sciences 11/2015; 112(46):201514748. DOI:10.1073/pnas.1514748112 · 9.67 Impact Factor
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    ABSTRACT: Lymphangiogenesis and concurrent angiogenesis are essential in supporting proliferation and survival of AIDS-related lymphomas, which are often metastatic. In vitro studies suggest a candidate angiogienic and lymphangiogenic factor encoded by HIV: the matrix protein p17. p17 accumulates in lymph nodes of patients even when they are undergoing higly active antiretroviral therapy. p17 has been found to affect immune cells, and recent data showed that a variant p17, called S75X, induces cell growth by triggering MAPK/ERK and PI3K/AKT pathways. We tested the in vivo angiogenic activity of p17 by injecting it in Matrigel plugs in nude mice. Plugs were retrieved 7 days after injection, and assessed macroscopically, and by light and confocal microscopy. Our data revealed that both reference and S75X variant p17 promote angiogenesis and lymphangiogenesis in vivo.. Our results suggest that the induction of angiogenesis and lymphangiogenesis by HIV-1 p17 may generate a favorable microenvironment that could trigger tumor growth and maintenance. Moreover, the presence of adipocytes infiltration observed at the histological level suggests a possible interplay between angiogenesis, lymphangiogenesis and adipogenesis. These findings offer new opportunities for the development of treatment strategies to combat HIV-related cancers. © FEMS 2015. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.
    Pathogens and Disease 09/2015; DOI:10.1093/femspd/ftv062 · 2.40 Impact Factor
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    ABSTRACT: HIV necessitates host factors for successful completion of its life cycle. Mammalian target of rapamycin (mTOR) is a conserved serine/threonine kinase that forms two complexes, mTORC1 and mTORC2. Rapamycin is an allosteric inhibitor of mTOR that selectively inhibits mTORC1. Rapamycin interferes with viral entry of CCR5 (R5)-tropic HIV and with basal transcription of the HIV LTR, potently inhibiting replication of R5 HIV but not CXCR4 (X4)-tropic HIV in primary cells. The recently developed ATP-competitive mTOR kinase inhibitors (TOR-KIs) inhibit both mTORC1 and mTORC2. Using INK128 as a prototype TOR-KI, we demonstrate potent inhibition of both R5 and X4 HIV in primary lymphocytes (EC50 < 50 nM), in the absence of toxicity. INK128 inhibited R5 HIV entry by reducing CCR5 levels. INK128 also inhibited both basal and induced transcription of HIV genes, consistent with inhibition of mTORC2, whose activity is critical for phosphorylation of PKC isoforms and, in turn, induction of NF-κB. INK128 enhanced the antiviral potency of the CCR5 antagonist maraviroc, and had favorable antiviral interactions with HIV inhibitors of reverse transcriptase, integrase and protease. In humanized mice, INK128 decreased plasma HIV RNA by >2 log10 units and partially restored CD4/CD8 cell ratios. Targeting of cellular mTOR with INK128 (and perhaps others TOR-KIs) provides a potential strategy to inhibit HIV, especially in patients with drug resistant HIV strains.
    Proceedings of the National Academy of Sciences 07/2015; 112(30):9412-7. DOI:10.1073/pnas.1511144112 · 9.67 Impact Factor
  • Robert C. Gallo ·
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    ABSTRACT: Human immunodeficiency virus (HIV) genome integration indicates that persistent sterilizing immunity will be needed for a successful vaccine candidate. This suggests a need for broad antibodies targeting the Env protein. Immunogens targeting gp120 have been developed that block infection in monkeys and mimic the modest success of the RV144 clinical trial in that protection is short-lived following a decline in antibody-depending cell-mediated cytotoxicity-like antibodies. Attempts to induce antibody persistence have been complicated by a loss of efficacy, presumably by increasing the number of HIV-target cells. The key seems to be achieving an immune balance. © The Author 2015. Published by Oxford University Press on behalf of the Infectious Diseases Society of America. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com.
    The Journal of Infectious Diseases 07/2015; 212(suppl 1). DOI:10.1093/infdis/jiv069 · 6.00 Impact Factor
  • Robert C. Gallo ·

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    ABSTRACT: A guiding principle for HIV vaccine design has been that cellular and humoral immunity work together to provide the strongest degree of efficacy. However, three efficacy trials of Ad5-vectored HIV vaccines showed no protection. Transmission was increased in two of the trials, suggesting that this vaccine strategy elicited CD4+ T-cell responses that provide more targets for infection, attenuating protection or increasing transmission. The degree to which this problem extends to other HIV vaccine candidates is not known. Here, we show that a gp120-CD4 chimeric subunit protein vaccine (full-length single chain) elicits heterologous protection against simian-human immunodeficiency virus (SHIV) or simian immunodeficiency virus (SIV) acquisition in three independent rhesus macaque repeated low-dose rectal challenge studies with SHIV162P3 or SIVmac251. Protection against acquisition was observed with multiple formulations and challenges. In each study, protection correlated with antibody-dependent cellular cytotoxicity specific for CD4-induced epitopes, provided that the concurrent antivaccine T-cell responses were minimal. Protection was lost in instances when T-cell responses were high or when the requisite antibody titers had declined. Our studies suggest that balance between a protective antibody response and antigen-specific T-cell activation is the critical element to vaccine-mediated protection against HIV. Achieving and sustaining such a balance, while enhancing antibody durability, is the major challenge for HIV vaccine development, regardless of the immunogen or vaccine formulation.
    Proceedings of the National Academy of Sciences 03/2015; 112(9):E992-E999. DOI:10.1073/pnas.1423669112 · 9.67 Impact Factor
  • Robert C. Gallo ·

    Transfusion 12/2014; 55(1). DOI:10.1111/trf.12935 · 3.23 Impact Factor
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    ABSTRACT: To target the HIV CD4i envelope epitope, we primed rhesus macaques with replicating Ad-rhFLSC (HIV-1BaLgp120 linked to macaque CD4 D1 and D2), with or without Ad-SIVgag and Ad-SIVnef. Macaques were boosted with rhFLSC protein. Memory T-cells in PBMC, bronchoalveolar lavage and rectal tissue, antibodies with neutralizing and ADCC activity, and Env-specific secretory IgA in rectal secretions were elicited. Although protective neutralizing antibody levels were induced, SHIVSF162P4 acquisition following rectal challenge was not prevented. Rapid declines in serum ADCC activity, Env-specific memory B cells in PBMC and bone marrow, and systemic and mucosal memory T cells were observed immediately post-challenge together with delayed anamnestic responses. Innate immune signaling resulting from persisting Ad replication and the TLR-4 booster adjuvant may have been in conflict and reoriented adaptive immunity. A different adjuvant paired with replicating Ad, or a longer post-prime interval allowing vector clearance before boosting might foster persistent T- and B-cell memory.
    Virology 12/2014; 471. DOI:10.1016/j.virol.2014.10.001 · 3.32 Impact Factor
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    George K Lewis · Anthony L DeVico · Robert C Gallo ·
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    ABSTRACT: The quest for a prophylactic AIDS vaccine is ongoing, but it is now clear that the successful vaccine must elicit protective antibody responses. Accordingly, intense efforts are underway to identify immunogens that elicit these responses. Regardless of the mechanism of antibody-mediated protection, be it neutralization, Fc-mediated effector function, or both, antibody persistence and appropriate T-cell help are significant problems confronting the development of a successful AIDS vaccine. Here, we discuss the evidence illustrating the poor persistence of antibody responses to Env, the envelope glycoprotein of HIV-1, and the related problem of CD4(+) T-cell responses that compromise vaccine efficacy by creating excess cellular targets of HIV-1 infection. Finally, we propose solutions to both problems that are applicable to all Env-based AIDS vaccines regardless of the mechanism of antibody-mediated protection.
    Proceedings of the National Academy of Sciences 10/2014; 111(44). DOI:10.1073/pnas.1413550111 · 9.67 Impact Factor

  • JAMA The Journal of the American Medical Association 07/2014; 312(4):442. DOI:10.1001/jama.2013.279636 · 35.29 Impact Factor
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    ABSTRACT: Background and aims Hydrogen sulfide (H2S), together with nitric oxide (NO) and carbon monoxide (CO), belongs to a family of endogenous signaling mediators termed “gasotransmitters”. Recent studies suggest that H2S modulates many cellular processes and it has been recognized to play a central role in inflammation, in the cardiovascular and nervous systems. By infecting monocytes/macrophages with Mycoplasma fermentans (M.F.), a well-known pro-inflammatory agent, we evaluated the effects of H2S. Methods M.F.-infected cells were analyzed by ELISA and real time RT-PCR to detect the M.F. effects on MCP-1 and on MMP-12 expression. The role of two different H2S donors (NaHS and GYY4137) on MF-infected cells was determined by treating infected cells with H2S and then testing the culture supernatants for MCP-1 and on MMP-12 production by ELISA assay. In order to identify the pathway/s mediating H2S- anti-inflammatory activity, cells were also treated with specific pharmaceutical inhibitors. Cytoplasmic and nuclear accumulation of NF-κB heterodimers was analyzed. Results We show that H2S was able to reduce the production of pro-inflammatory cytokine MCP-1, that was induced in monocytes/macrophages during M.F. infection. Moreover, MCP-1 was induced by M.F. through Toll-like receptor (TLR)-mediated nuclear factor-κB (NF-κB) activation, as demonstrated by the fact that TLR inhibitors TIRAP and MyD88 and NF-κB inhibitor IKK were able to block the cytokine production. In contrast H2S treatment of M.F. infected macrophages reduced nuclear accumulation of NF-κB heterodimer p65/p52. Conclusions Our data demonstrate that under the present conditions H2S is effective in reducing Mycoplasma-induced inflammation by targeting the NF-κB pathway. This supports further studies for possible clinical applications.
    Journal of Translational Medicine 05/2014; 12(1):145. DOI:10.1186/1479-5876-12-145 · 3.93 Impact Factor
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    ABSTRACT: Shortly after the discovery of human herpesvirus 6 (HHV-6), two distinct variants, HHV-6A and HHV-6B, were identified. In 2012, the International Committee on Taxonomy of Viruses (ICTV) classified HHV-6A and HHV-6B as separate viruses. This review outlines several of the documented epidemiological, biological, and immunological distinctions between HHV-6A and HHV-6B, which support the ICTV classification. The utilization of virus-specific clinical and laboratory assays for distinguishing HHV-6A and HHV-6B is now required for further classification. For clarity in biological and clinical distinctions between HHV-6A and HHV-6B, scientists and physicians are herein urged, where possible, to differentiate carefully between HHV-6A and HHV-6B in all future publications.
    Archives of Virology 11/2013; 159(5). DOI:10.1007/s00705-013-1902-5 · 2.39 Impact Factor

  • Conference on AIDS Vaccine; 11/2013
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    ABSTRACT: Human Immunodeficiency Virus Type I (HIV-1) infection is associated with a high incidence of B-cell lymphomas. The role of HIV in these lymphomas is unclear and currently there are no valid in vivo models for better understanding HIV-related lymphomagenesis. Transgenic (Tg) 26 mice have a 7.4-kb pNL4-3 HIV-1 provirus lacking a 3.1-kb sequence encompassing parts of the gag-pol region. Approximately 15% of these HIV Tg mice spontaneously develop lymphoma with hallmark pre-diagnostic markers including skin lesions, diffuse lymphadenopathy and an increase in pro-inflammatory serum cytokines. Here we describe the phenotypic and molecular characteristics of the B cell leukemia/lymphoma in the Tg mice. The transformed B cell population consists of CD19+pre-BCR+CD127+CD43+CD93+ precursor B cells. The tumor cells are clonal and characterized by an increased expression of several cellular oncogenes. Expression of B cell-stimulatory cytokines IL-1beta, IL-6, IL-10, IL-12p40, IL-13 and TNFalpha and HIV proteins p17, gp120 and nef were elevated in the Tg mice with lymphoma. Increased expression of HIV proteins and the B-cell stimulatory factors is consistent with the interpretation that one or more of these factors play a role in lymphoma development. The lymphomas share many similarities with those occurring in HIV/AIDS+ patients and may provide a valuable model for understanding AIDS-related lymphomagenesis and elucidating the role played by HIV-1.
    Retrovirology 08/2013; 10(1):92. DOI:10.1186/1742-4690-10-92 · 4.19 Impact Factor
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    ABSTRACT: Recent identification of large numbers of new broadly neutralizing antibodies (bnAbs) against HIV-1 is leading a vaccine path based on their epitopes. However, majority of the newly identified bnAbs have apparent unusually high levels of mutation, which raises a high bar for a vaccine to generate this type of Ab response. Here we show by phylogenetic analysis that these highly mutated bnAbs cluster into two families of VH genes that are distant from known VH germline genes. It is recognized that the number of human Ab germline genes is not always the same due to genetic polymorphism. Our studies on diversity of VH germline genes also find that diversity of VH germline genes is common. These observations indicate that the diversity of Ab germline genes may limit the induction of these bnAbs at the population level. Here we describe a new potent bnAb, N60-B1.1 that neutralizes 40% of a panel of 118 tier 2,3 viruses with an average IC50 of 0.44 ug/ml. The neutralization pattern of N60-B1.1 is complementary to other bnAbs in that it potently neutralizes viruses that are more resistant to these other antibodies. This bnAb is encoded by VH4-39*07 that is somatically mutated 13.3% at the nucleotide level, which is within the normal somatic mutation rate for vaccine induced antibodies. It uses a single point mutated light chain of germline (CDRL3) VK3-15*01. Theoretically, the induction of "N60-B1.1-like" bnAb will not be limited by the somatic mutation bottleneck that is required for other bnAbs against HIV-1. Therefore, rational design of Env immunogens that preferentially expose "N60-B1.1-like" epitopes to elicit bnAb responses is a promising direction for the development of a protective HIV-1 vaccine.
    JAIDS Journal of Acquired Immune Deficiency Syndromes 04/2013; 62:S53. DOI:10.1097/01.qai.0000429244.16910.d3 · 4.56 Impact Factor
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    ABSTRACT: The HIV-1 envelope glycoprotein (Env) undergoes conformational transitions consequent to CD4 binding and coreceptor engagement during viral entry. The physical steps in this process are becoming defined, but less is known about their significance as targets of antibodies potentially protective against HIV-1 infection. Here we probe the functional significance of transitional epitope exposure by characterizing 41 human mAbs specific for epitopes exposed on trimeric Env after CD4 engagement. These mAbs recognize three epitope clusters: cluster A, the gp120 face occluded by gp41 in trimeric Env; cluster B, a region proximal to the coreceptor-binding site (CoRBS) and involving the V1/V2 domain; and cluster C, the coreceptor-binding site. The mAbs were evaluated functionally by antibody-dependent, cell-mediated cytotoxicity (ADCC) and for neutralization of Tiers 1 and 2 pseudoviruses. All three clusters included mAbs mediating ADCC. However, there was a strong potency bias for cluster A, which harbors at least three potent ADCC epitopes whose cognate mAbs have electropositive paratopes. Cluster A epitopes are functional ADCC targets during viral entry in an assay format using virion-sensitized target cells. In contrast, only cluster C contained epitopes that were recognized by neutralizing mAbs. There was significant diversity in breadth and potency that correlated with epitope fine specificity. In contrast, ADCC potency had no relationship with neutralization potency or breadth for any epitope cluster. Thus, Fc-mediated effector function and neutralization coselect with specificity in anti-Env antibody responses, but the nature of selection is distinct for these two antiviral activities.
    Proceedings of the National Academy of Sciences 12/2012; 110(1). DOI:10.1073/pnas.1217609110 · 9.67 Impact Factor
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    Retrovirology 05/2012; 9(1). DOI:10.1186/1742-4690-9-S1-P35 · 4.19 Impact Factor
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    ABSTRACT: The HIV-1 envelope glycoprotein (Env) undergoes ordered conformational transitions after CD4 binding and co-receptor engagement during viral entry. While the physicochemical steps of viral entry are becoming defined, less is known about their immunochemical correlates and their roles as targets of protective antibodies. We describe studies that define the functional significance of epitope exposure during the first step of viral entry, the binding of gp120 to CD4. A panel of 41 human monoclonal antibodies (mAbs) were isolated that recognize epitopes which become exposed on trimeric Env only after CD4 engagement. These mAbs recognize clusters of epitopes mapping to three regions of gp120: a. Cluster A, the domain of gp120 occluded by interaction with gp41; b. Cluster B, a region proximal to the classical co-receptor binding site (CoRBS) involving the V1/V2 region; and Cluster C, the CoRBS. The mAbs were characterized for neutralization of Tier 1 and Tier 2 pseudoviruses and by antibody dependent cell mediated cytotoxicity (ADCC). mAbs recognizing all three clusters mediated ADCC but there was a strong bias in potency for mAbs that recognize Clusters A and B. Surprisingly, ADCC potency correlated inversely with CDR-H3 length but not with somatic hypermutation. By contrast, mAbs binding Cluster C epitopes were neutralizing but there was significant diversity in breadth and potency that correlated with epitope fine specificity and somatic hypermutation. ADCC potency did not correlate with neutralization breadth or potency. Thus, both neutralization and Fc-mediated effector function are co-selected with specificity but the nature of selection is distinct for these two anti-viral activities.
    JAIDS Journal of Acquired Immune Deficiency Syndromes 04/2012; 59:45. DOI:10.1097/01.qai.0000413731.29857.f7 · 4.56 Impact Factor
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    ABSTRACT: T-cell-derived soluble factors that inhibit both X4 and R5 HIV are recognized as important in controlling HIV. Whereas three β chemokines, regulated-on-activation normal T-cell expressed and secreted (RANTES), macrophage inflammatory protein (MIP)-1α, and MIP-1β, account for the suppression of R5 HIV by blockade of HIV entry, the major components responsible for the inhibition of X4 HIV strains have not been identified previously. We identify these factors primarily as a mixture of three β chemokines [macrophage-derived chemokine (MDC), thymus and activation-regulated chemokine (TARC), and I-309] and two RNases (angiogenin and RNase 4) of lesser potency and show that in a clade B population, some correlate with clinical status and are produced by both CD4(+) and CD8(+) T cells (chemokines, angiogenin) or only by CD8(+) T cells (RNase 4). The antiviral mechanisms of these HIV X4-suppressive factors differ from those of the previously described HIV R5-suppressive β chemokines.
    Proceedings of the National Academy of Sciences 03/2012; 109(14):5411-6. DOI:10.1073/pnas.1202240109 · 9.67 Impact Factor

Publication Stats

81k Citations
11,622.22 Total Impact Points


  • 1996-2015
    • University of Maryland, Baltimore
      • • Institute of Human Virology
      • • Department of Medicine
      Baltimore, Maryland, United States
    • Cancer Research Institute
      New York, New York, United States
  • 1999-2014
    • Institute of Human Virology
      Maryland City, Maryland, United States
  • 1969-2007
    • National Cancer Institute (USA)
      • • Laboratory of Cell Biology
      • • Basic Research Laboratory
      Maryland, United States
  • 2005
    • University Hospital Frankfurt
      Frankfurt, Hesse, Germany
    • Bernhard Nocht Institute for Tropical Medicine
      Hamburg, Hamburg, Germany
  • 2002
    • University of Baltimore
      Baltimore, Maryland, United States
  • 1999-2001
    • Loyola University Maryland
      Baltimore, Maryland, United States
  • 2000
    • Johns Hopkins Medicine
      • Department of Neurology
      Baltimore, Maryland, United States
    • University of Maryland Medical Center
      • Institute for Human Virology
      Baltimore, Maryland, United States
  • 1997
    • Georgetown University
      Washington, Washington, D.C., United States
  • 1996-1997
    • San Raffaele Scientific Institute
      Milano, Lombardy, Italy
  • 1967-1997
    • National Institutes of Health
      • • Basic Research Laboratory
      • • Laboratory of Cell Biology
      • • Branch of Surgery
      • • Branch of Cell Biology
      • • Laboratory of Pathology
      Bethesda, MD, United States
  • 1995
    • Johns Hopkins University
      Baltimore, Maryland, United States
    • Karolinska University Hospital
      Tukholma, Stockholm, Sweden
    • National Heart, Lung, and Blood Institute
      • Hematology Branch
      Bethesda, MD, United States
  • 1982-1993
    • NCI-Frederick
      Фредерик, Maryland, United States
    • Moncrief Cancer Institute
      Fort Worth, Texas, United States
  • 1992
    • University of California, San Diego
      San Diego, California, United States
    • Université de Montréal
      • Faculty of Medicine
      Montréal, Quebec, Canada
    • University of Southern California
      Los Angeles, California, United States
  • 1990-1992
    • Kensington College
      Kensington, Connecticut, United States
    • Università degli Studi di Torino
      Torino, Piedmont, Italy
    • Institut Jean-Godinot
      Rheims, Champagne-Ardenne, France
  • 1991
    • National Institute of Allergy and Infectious Diseases
      • Laboratory of Immunoregulation
      Maryland, United States
  • 1989
    • University of Cologne
      • Institute of Pathology
      Köln, North Rhine-Westphalia, Germany
  • 1987-1989
    • Pierre and Marie Curie University - Paris 6
      • Laboratoire de Physiologie Cellulaire et Moléculaire des Plantes (PCMP)
      Lutetia Parisorum, Île-de-France, France
    • Washington University in St. Louis
      • Division of Hematology and oncology
      Saint Louis, MO, United States
  • 1985-1989
    • University of Tampere
      • Institute of Biomedical Sciences
      Tampere, Western Finland, Finland
    • Lund University
      Lund, Skåne, Sweden
    • Vrije Universiteit Brussel
      Bruxelles, Brussels Capital Region, Belgium
    • Kumamoto University
      Kumamoto, Kumamoto, Japan
    • New York Blood Center
      New York, New York, United States
    • Dana-Farber Cancer Institute
      Boston, Massachusetts, United States
    • University of Helsinki
      • Department of Virology
      Helsinki, Uusimaa, Finland
    • National Eye Institute
      Maryland, United States
    • Centre Hospitalier Universitaire Saint-Pierre
      Bruxelles, Brussels Capital, Belgium
    • Walter Reed Army Institute of Research
      Silver Spring, Maryland, United States
    • Massachusetts General Hospital
      • Pediatric Infectious Disease Unit
      Boston, Massachusetts, United States
  • 1988
    • Institut Pasteur
      • Department of Virology
      Lutetia Parisorum, Île-de-France, France
  • 1987-1988
    • Karolinska Institutet
      Solna, Stockholm, Sweden
  • 1985-1987
    • Sapienza University of Rome
      Roma, Latium, Italy
  • 1984-1987
    • Duke University Medical Center
      • • Department of Surgery
      • • Department of Medicine
      Durham, NC, United States
    • University of Pennsylvania
      • Department of Medicine
      Filadelfia, Pennsylvania, United States
  • 1986
    • Columbia University
      • College of Physicians and Surgeons
      New York, New York, United States
  • 1982-1985
    • Kyoto University
      • • Institute for Virus Research
      • • Department of Microbiology
      Kioto, Kyōto, Japan
  • 1983
    • Duke University
      Durham, North Carolina, United States
    • The University of the West Indies at Mona
      • Department of Pathology
      Kingston, Kingston, Jamaica
  • 1981
    • The Rockefeller University
      New York, New York, United States
  • 1974
    • Princeton University
      Princeton, New Jersey, United States