Kliniken & Institute … Institute Zentrum für… Department of Virology … Research Kräusslich

Research Group Kräusslich

Hans-Georg Kräusslich is speaker of the SFB1129 and chairman of the DZIF executive board.

You can find our lab on the 3rd floor of the CIID (INF344).

Projects

Research projects in our group address different aspects of retroviral and influenza virus (IAV) biology. A long-term interest of the group is the formation and architecture of the infectious human immunodeficiency virus (HIV) particle. A major current focus in the lab is the study of  entry and post-entry stages in the life cycle of HIV-1 and murine leukemia virus and the role of innate immune responses. We combine conventional and super-resolution microscopy as well as correlative-light and electron microscopy (CLEM) to study the composition and architecture of entering subviral complexes and the interaction with cellular proteins and structures. Other projects address the role of lipids for virus assembly and cell entry, the use of CRISP/Cas based approaches for HIV-1 elimination, and the entry and spread of influenza virus in complex cell systems.

Morphogenesis and structure of HIV particles

Tomogram of HIV particles (red) budding at the plasma membrane (blue)

Assembly and budding of human immunodeficiency virus (HIV) is directed by the main structural polyprotein Gag and occurs at the plasma membrane of the infected cell. The virus is initially released as immature non-infectious particle consisting of mostly uncleaved Gag polyproteins. The immature virion consists of approximately 2500 Gag molecules arranged as spherical protein shell. Particle maturation occurs after proteolytic processing of Gag at five different cleavage sites, which is mediated by the virus-encoded, virion-associated protease (PR). Maturation leads to disassembly of the immature Gag layer, followed by a second assembly stage forming the mature cone-shaped capsid that incorporates the condensed viral genome associated with replication proteins.

The assembly of immature particles requires only the viral Gag polyprotein and can be mimicked in vitro using bacterially expressed purified Gag-derived proteins. We have developed in vitro assembly systems to analyze the molecular architecture of capsid assemblies, to study the effect of mutations on mature and immature particle formation and identify inhibitors of HIV assembly. These studies are complemented by analyses of HIV particle formation in tissue culture.

We employ structural analyses including transmission EM, cryo-EM and tomography to obtain detailed three-dimensional images of mature and immature virions, as well as viral budding sites, of wild-type and mutant HIV. These provide a better understanding of the mechanisms and protein interfaces governing assembly and maturation.


 

Post-entry stages of retroviral replication

Delivery of the genome-containing retroviral capsid into the cytoplasm of a newly infected cell is followed by reverse transcription of the viral RNA and transport of the resulting cDNA to the host cell DNA, where the genetic information of the virus is integrated. These early post-entry replication steps occur within poorly characterized subviral complexes termed reverse-transcription and pre-integration complexes (RTC/PIC). Increasing evidence indicates that the viral capsid plays a central role throughout this replication phase. 

A detailed understanding of post-entry is hampered by the fact that reverse transcription, intracellular transport and capsid uncoating are tightly intertwined. Furthermore, numerous host cell dependency and restriction factors affect these processes in a cell type dependent manner. Finally, there are fundamental differences not only between different types of host cells, but also between different retroviruses. While many retroviruses (e.g. moloney leukemia virus, MLV) depend on cell division to gain access to the host cell genome, lentiviruses, e.g. HIV-1, can enter the intact nucleus through nuclear pores.

Our work on retroviral post-entry comprises a number of different projects, in which we

  • characterize the composition and structure of retroviral replication complexes in different cells and at different intracellular localizations
  • investigate the function of host cell dependency (e.g., CPSF6, Nup153) and restriction factors that interact with the incoming viral capsid and of cellular sensors (e.g., cGAS, TREX1) that detect the viral cDNA
  • assess the role of capsid stability in post-entry processes
  • compare replication pathways and cellular immune responses in HIV-1 and MLV infected cells.

For this, we combine advanced labeling technologies (e.g., EdU-click labeling of viral DNA, 3D FISH, ANCHOR visualization) with state-of-the art microscopy (STED nanoscopy, correlative light and electron microscopy, (cryo)electron tomography, live cell imaging), molecular biological (e.g., digital droplet PCR), virological and biochemical approaches. In these projects, we collaborate with different groups within the SFB1129 and SPP1923.

Post-entry steps in retroviral replication. The retroviral capsid which houses the viral RNA is released in the cytoplasm of the infected cell. The capsid has to navigate through a hostile cytoplasmic environment while the RNA genome is reverse transcribed into DNA. Numerous host cell factors can target viral replication complexes. We are particularly interested in (i) cGAS, a component of the innate immune system that detects the presence of viral DNA (ii) TREX1 digests abortive viral cDNA thus downregulating the immune response to MLV and HIV-1 infection, (iii) NONO, that binds directly to capsid and is essential for cGAS activation and relocalization to the nucleus.

Role of lipids in HIV replication

HIV is an enveloped virus. Its protein capsid is surrounded by a lipid envelope, which is derived from the host cell membrane in the viral budding process. During infection of new host cells, this lipid envelope fuses to the cellular plasma membrane. Thus, lipids are involved in virus entry and egress, and they may play functional roles in viral protein composition, particle stability and infectivity. However, unlike viral proteins, viral lipids and their functional role a poorly understood.

In collaboration with Britta Brügger we have determined the lipidome of  HIV using mass spectroscopy and biochemical approaches. We are currently analyzing the influence of host cells and viral proteins on the lipid compostion of the envelope and study the influence of lipid composition on the properties of the virus.

In order to study the lipid and protein organization at HIV-1 assembly sites, we have developed a system that allows us to recruit the viral structural protein Gag to the plasma membrane at a defined time point. Using clickable lipid analogs and STED nanoscopy we investigate the (re)distribution of distinct lipids during the viral assembly process.

CRISPR/Cas based approaches for HIV-1 elimination

Current antiretroviral therapy (cART) can prevent destruction of the immune system of HIV-1 infected patients and protects from developing AIDS disease. However, drug treatment does not cure the infection. HIV-1 integrates its genetic information into the host genome and can thus not be eliminated from the organism once the infection is established. Interruption of therapy thus results in renewed virus production from latent reservoirs.

Within this project we aim at fully eradicating HIV by combining state-of-the art gene delivery and genome engineering technologies. In collaboration with the group of Dirk Grimm, we develop T cell specific viral gene transfer vectors and use them to express components of the CRISPR/Cas system in HIV-infected cells. CRISPR/Cas can be targeted to cleave and modify a desired DNA sequence. By directing the machinery to the viral genome we predict that we can inactivate the pathogenic sequences, thereby curing the infected cells (and, eventually, patients). Our goal is to provide proof-of-concept for the efficacy of this strategy in increasingly complex models of HIV infection, from acutely infected T-cell lines and chronically infected primary patient cells to a humanized small animal model of persistent HIV infection.

Spread of influenza virus in human lung organoids

Influenza virus is a major human pathogen that affects roughly 10% of the world population each year. Despite intense research efforts, currently available vaccines and virostatics have significant limitations. Our group wants to obtain a better understanding of the formation and spread of influenza virus. While most studies to date were carried out using lab adapted influenza variants that form small spherical particles, most influenza viruses from patient samples appear to be micrometer long filaments. How these filamentous particles are formed and how they are taken up into the next host cell is currently not understood.  

For our studies we develop fluorescently labeled influenza virus derivatives that allow us to analyze replication and spread of  spheroidal and filamentous particles by live cell imaging and superresolution microscopy. In order to investigate influenza virus particle formation and spread in a complex environment, we have established culture systems for human lung organoids. Organoids are millimeter sized three-dimensional microstructures which can be grown from various types of stem cells. They comprise a variety of specialized cells typical for a specific organ and thus mimick the complex environment that the virus encounters in vivo.

Using this approach, complemented by biochemical and virological methods, we address questions as

  • How do spheroidal and filamentous particles differ with respect to spread in 3D environments?
  • Is particle release necessary for cell-cell transmission of infection?
  • How are filamentous particles taken up into the host cell?
  • How does interferon signalling influence the spread of influenza virus?
  • What is the role of lipids in the viral assembly process?
Human lung organoid. Cell nuclei (DraQ5) and the mucin 1 transmembrane protein are stained for visualization.

mi(cro) RNAs in HIV-1 infection

miRNAs are small, noncoding RNAs involved in gene regulation. They are frequently dysregulated in human diseases and in infected cells, so that their expression pattern may serve as a signature to distinguish between healthy and pathological states. Furthermore, miRNAs are apparently secreted from cells into easily accessible body fluids (e.g., blood). Comparing the miRNAs expression pattern in cells and body fluids between patients and healthy individuals can thus yield novel biomarkers for monitoring infections.

In this project, which is carried out in collaboration with the group of Dirk Grimm, we study how HIV-1, infection alters the miRNA profiles detected in human blood. We used microarrays to compare a subset of miRNAs in HIV-1-infected individuals and healthy controls. Data from this pilot study showed that HIV-1 infection triggers a substantial dysregulation of miRNA expression in blood cells and especially in cell-free serum. For additional validation, we re-analyze our samples by using a novel approach for detection and quantification of miRNAs that is based on "droplet digital PCR" (ddPCR) technology. The combined results from our prior and ongoing work should yield a comprehensive picture of the miRNA alterations that occur during HIV-1 infection.

Group members

Prof. Dr. med. Hans-Georg Kräusslich,
E-Mail
Phone: +49 6221 56-5001
Fax: +49 6221 56-5003

 

Dr. David Bejarano, postdoc
E-Mail
Tel: +49 6221 56-1323

Sarah Bunten, PhD student
e-mail
Tel: +49 6221 56-1324

Dr. Kathleen Börner, scientific associate
e-mail
Tel: +49 6221 56-1323

Bärbel Glass, lab manager
E-Mail
Phone: +49 6221 56-1323

Anke-Mareil Heuser, technician
E-Mail
Phone: +49 6221 56-1323

Tina Holdt, technician
e-mail
Tel: +49 6221 56-1323

Dr. Vibor Laketa,
Head of the Infectious Diseases Imaging Platform
IDIP
E-Mail
Phone: +49 6221 56-34410

Thorsten Müller, PhD student
E-mail
Tel: +49 6221 56-1324

Tamara Naumoska, PhD student
e-mail
Tel: +49 6221 56-1323

Djordje Salai, PhD student
e-mail
Tel: +49 6221 56-1323

Jian Song, PhD student
e-mail
Tel: +49 6221 56-1323

Vera Sonntag-Buck, Technician
e-mail
Phone: +49 6221 56-1323

Dr. Vojtech Zila, postdoc
E-Mail
Tel: +49 6221 56-1323

Former lab members

Yvonne Affram,PhD student
Dr. Hisashi Akiyama, postdoc
Anne Assmus, diploma student
Vanda Bartonova, PhD student

Daniel Beyer, PhD student
Dr. Jochen Bodem, postdoc
Jens Bohne, PhD student

Lorenzo Bulli, PhD student

Robin Burk, PhD student, postdoc
Luis Castillo, PhD student
Dr. Jakub Chojnacki, postdoc
Ellen Collenberg, MD student
Jessica Daecke, PhD student
Christine Engeland, MD student
Eva Gottwein, PhD student
Anja Habermann, technician
Isabel Hagmann, technician
Janina Hanne, PhD student
Johannes Hermle, PhD student
Nikoas Herold, MD student
Volker Herrmann, PhD Student
Dr. Katharina Höhn, postdoc
Dr. Nuria Izquierdo, guest scientist
Stefanie Jäger, PhD student
Dr. Jessica Janus, postdoc
Heiko Keller, guest scientist
Peter Koch, PhD student

Dr. Susann Kummer, postdoc

Juliane Kutzner, PhD student
Dr. Maik Lehmann, postdoc
Dr. Maier Lorizate, postdoc
Ivonne Morales, PhD student
Vanessa Mrosek, MD student
Kerstin Müller, diploma Student

Frauke Mücksch, PhD student
PD Dr. Walter Muranyi, research associate
Manuela Nickl, PhD student
Bianca Nouvertne, PhD student
Heike Oberwinkler, technician
Martin Obr, PhD student
Dr. Ke Peng, postdoc
Benjamin Radestock, PhD student
Dr. Sandra Reuter, postdoc
Kanokporn Sathiandee, PhD student
Michaela Schanne, PhD student
Sarah Stauffer, Masters student
Jana Sticht, PhD student
Denis Manga Tebit, PhD student
Fabrice Tiba, PhD student
Max von Au, MD student
Sonja Welsch, PhD student
Dr. Marcela Wildova, postdoc

Selected publications

Complete Publication List (PubMed)

Zila, V., Müller, T.G., Laketa, V., Müller, B. and Kräusslich, H.G. (2019). Analysis of CA Content and CPSF6 Dependence of Early HIV-1 Replication Complexes in SupT1-R5 Cells. MBio, doi 10.1128/mBio.02501-19

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Bejarano, D.A., Peng, K., Laketa, V., Börner, K., Jost, K.L., Lucic, B., Glass, B., Lusic, M., Müller, B., and Kräusslich, H.G. (2019). HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the Nuclear Pore Complex. eLife, e41800.

Mattei S., Tan A, Glass B, Müller B., Kräusslich H.G., and Briggs J.A.G. (2018) High-resolution structures of HIV-1 Gag cleavage mutants determine structural switch for virus maturation. Proc Natl Acad Sci USA. https://doi.org/10.1073/pnas.181123711.5
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Mücksch F, Laketa V, Müller B, Schultz C, Kräusslich HG (2017) Synchronized HIV assembly by tunable PIP2 changes reveals PIP2 requirement for stable Gag anchoring. Elife. pii: e25287. doi: 10.7554/eLife.25287.
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Mattei S, Glass B, Hagen WJ, Kräusslich HG, Briggs JA. (2016). The structure and flexibility of conical HIV-1 capsids determined within intact virions.
Science 354(6318):1434-1437.
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Hanne J,  Göttfert F, Schimer J, Anders-Össwein M, Konvalinka J, Engelhardt J, Müller B, Hell SW,  Kräusslich HG (2016). Stimulated Emission Depletion Nanoscopy Reveals Time-Course of Human Immunodeficiency Virus Proteolytic Maturation . ACS Nano, in press
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Schur FK, Obr M, Hagen WJ, Wan W, Jakobi AJ, Kirkpatrick JM, Sachse C, Kräusslich HG, Briggs JA (2016) An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation.
Science 353(6298):506-8.
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Hanne J, Zila V, Heilemann M, Müller B, Kräusslich HG.(2016) Super-resolved insights into human immunodeficiency virus biology. FEBS Lett. 590(13):1858-76.
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FEBS Letters Special Issue (2016) Integrative analysis of pathogen replication and spread. http://febs.onlinelibrary.wiley.com/hub/issue/10.1111/feb2.2016.590.issue-13/
Konvalinka, J., Kräusslich, H.G.***, and Müller, B. (2015). Retroviral proteases and their roles in virion maturation. Virology.  doi: 10.1016/j.virol.2015.03.021.

Schimer J, Pavova M, Anders M, Pachl P, Sacha P, Cigler P, Weber J, Majer P, Rezacova P, Kräusslich HG, Müller B***, Konvlinka J***, (2015). Triggering HIV polyprotein processing inside virions by rapid photodegradation of a tight-binding photodestructable protease Inhibitor. Nature Communications 6:6461

Peng K, Muranyi W., Glass B, Laketa V, Yant SR, Tsai L, Cihlar T, Müller B, Kräusslich, HG. (2014) Quantitative microscopy of functional HIV post-entry complexes reveals association of replication with the viral capsid. eLife 2014 10.7554/eLife.04114

Herold N, Anders-Ößwein M, Glass B, Eckhardt M, Müller B, Kräusslich HG. (2014) HIV-1 Entry in SupT1-R5, CEM-ss, and Primary CD4+ T Cells Occurs at the Plasma Membrane and Does Not Require Endocytosis. J Virol. 88:13956-70.

Schur, F.K.M., Hagen, W.J.H., Rumlová, M., Ruml, T., Müller, B., Kräusslich, H.G., and Briggs, J.A.G. (2014) The structure of the immature HIV-1 capsid in intact . virus particles at 8.8 Å resolution. Nature. 2014 Nov 2. doi: 10.1038/nature13838.

Izquierdo-Useros N, Lorizate M, Puertas MC, Rodriguez-Plata MT, Zangger N, Erikson E, Pino M, Erkizia I, Glass B, Clotet B, Keppler OT, Telenti A, Kräusslich HG, Martinez-Picado J. (2013) Siglec-1 is a novel dendritic cell receptor that mediates HIV-1 trans-infection through recognition of viral membrane gangliosides. PLoS Biol. 2012;10(12):e1001448.

Muranyi, W., S. Malkusch, B. Müller, M. Heilemann, and H. G. Kräusslich (2013) Super-resolution Microscopy Reveals Specific Recruitment of HIV-1 Envelope Proteins to Viral Assembly Sites dependent on the Envelope C-Terminal Tail.
PLoS Pathog, in press.

Chojnacki J, Staudt T, Glass B, Bingen P, Engelhardt J, Anders M, Schneider J, B. M, Hell S, Kräusslich HG (2012) Maturation Dependent HIV-1 Surface Protein Redistribution Revealed by Fluorescence Nanoscopy. Science 2012, 338:524-528.

Izquierdo-Useros, N., Lorizate, M., Contreras, F.X., Rodriguez-Plata, M.T., Glass, B., Erkizia, I., Prado, J.G., Casas, J., Fabrias, G., Kräusslich, H.G., et al. (2012). Sialyllactose in viral membrane gangliosides is a novel molecular recognition pattern for mature dendritic cell capture of HIV-1. PLoS biology 10, e1001315.

Radestock, B., Morales, I., Rahman, S.A., Radau, S., Glass, B., Zahedi, R.P., Müller, B., and Kräusslich, H.G. (2012). Comprehensive Mutational Analysis Reveals p6Gag Phosphorylation to be Dispensable for HIV-1 Morphogenesis and Replication. Journal of virology.

Geis, S., Prifert, C., Weissbrich, B., Lehners, N., Egerer, G., Eisenbach, C., Buchholz, U., Aichinger, E., Dreger, P., Neben, K., et al. (2012). Molecular Characterization of a Respiratory Syncytial Virus (RSV) Outbreak in a Hematology Unit, Heidelberg, Germany. Journal of clinical microbiology.

Sundquist, W.I., and Krausslich, H.G. (2011). HIV-1 Assembly, Budding, and Maturation. Cold Spring Harbor perspectives in medicine 2, a006924.

Lorizate, M. and Krausslich, H.G. Role of Lipids in Virus Replication. Cold Spring Harbor perspectives in biology. 2011. http://cshperspectives.cshlp.org/cgi/reprint/cshperspect.a004820v1.pdf?ijkey=k65EtMzXzCFRfLs&keytype=finite

Briggs JA, Kräusslich HG. (2011) The molecular architecture of HIV. J Mol Biol. 2011 Jul 22;410(4):491-500J Mol Biol. 410(4):491-500

von Kleist L, Stahlschmidt W, Bulut H, Gromova K, Puchkov D, Robertson MJ, MacGregor KA, Tomlin N, Pechstein A, Chau N, Chircop M, Sakoff J, von Kries JP, Saenger W, Kräusslich HG, Shupliakov O, Robinson PJ, McCluskey A, Haucke V. (2011) Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition.Cell 146(3):471-84.

Baumgartel, V., Ivanchenko, S., Dupont, A., Sergeev, M., Wiseman, P.W., Krausslich, H.G., Brauchle, C., Muller, B., and Lamb, D.C. 2011. Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component. Nature cell biology 13(4): 469-474.

Carlson, L.A., de Marco, A., Oberwinkler, H., Habermann, A., Briggs, J.A., Krausslich, H.G., and Grunewald, K. 2010. Cryo electron tomography of native HIV-1 budding sites. PLoS pathogens 6(11): e1001173.

de Marco, A., Muller, B., Glass, B., Riches, J.D., Krausslich, H.G., and Briggs, J.A. 2010. Structural analysis of HIV-1 maturation using cryo-electron tomography. PLoS pathogens 6(11): e1001215.

Habermann, A., Krijnse-Locker, J., Oberwinkler, H., Eckhardt, M., Homann, S., Andrew, A., Strebel, K., and Krausslich, H.G. 2010. CD317/tetherin is enriched in the HIV-1 envelope and downregulated from the plasma membrane upon virus infection. Journal of virology 84(9): 4646-4658.

Ivanchenko, S., Godinez, W.J., Lampe, M., Krausslich, H.G., Eils, R., Rohr, K., Brauchle, C., Muller, B., and Lamb, D.C. 2009. Dynamics of HIV-1 assembly and release. PLoS pathogens 5(11): e1000652.

Koch, P., Lampe, M., Godinez, W.J., Muller, B., Rohr, K., Krausslich, H.G., and Lehmann, M.J. 2009. Visualizing fusion of pseudotyped HIV-1 particles in real time by live cell microscopy. Retrovirology 6: 84.

Lorizate, M., Brugger, B., Akiyama, H., Glass, B., Muller, B., Anderluh, G., Wieland, F.T., and Krausslich, H.G. 2009. Probing HIV-1 membrane liquid order by Laurdan staining reveals producer cell-dependent differences. The Journal of biological chemistry 284(33): 22238-22247.

Muller, B., Anders, M., Akiyama, H., Welsch, S., Glass, B., Nikovics, K., Clavel, F., Tervo, H.M., Keppler, O.T., and Krausslich, H.G. 2009. HIV-1 Gag processing intermediates trans-dominantly interfere with HIV-1 infectivity. The Journal of biological chemistry 284(43): 29692-29703.

Pongratz, C., Yazdanpanah, B., Kashkar, H., Lehmann, M.J., Krausslich, H.G., and Kronke, M. Selection of potent non-toxic inhibitory sequences from a randomized HIV-1 specific lentiviral short hairpin RNA library. PloS one 5(10): e13172.

Rezacova, P., Pokorna, J., Brynda, J., Kozisek, M., Cigler, P., Lepsik, M., Fanfrlik, J., Rezac, J., Grantz Saskova, K., Sieglova, I., Plesek, J., Sicha, V., Gruner, B., Oberwinkler, H., Sedlacek, J., Krausslich, H.G., Hobza, P., Kral, V., and Konvalinka, J. 2009. Design of HIV protease inhibitors based on inorganic polyhedral metallacarboranes. Journal of medicinal chemistry 52(22): 7132-7141.

Tebit, D.M., Lobritz, M., Lalonde, M., Immonen, T., Singh, K., Sarafianos, S., Herchenroder, O., Krausslich, H.G., and Arts, E.J. Divergent evolution in reverse transcriptase (RT) of HIV-1 group O and M lineages: impact on structure, fitness, and sensitivity to nonnucleoside RT inhibitors. Journal of virology 84(19): 9817-9830.

Tebit, D.M., Sangare, L., Tiba, F., Saydou, Y., Makamtse, A., Somlare, H., Bado, G., Kouldiaty, B.G., Zabsonre, I., Yameogo, S.L., Sathiandee, K., Drabo, J.Y., and Krausslich, H.G. 2009. Analysis of the diversity of the HIV-1 pol gene and drug resistance associated changes among drug-naive patients in Burkina Faso. Journal of medical virology 81(10): 1691-1701.

Welsch, S., Groot, F., Krausslich, H.G., Keppler, O.T., and Sattentau, Q. 2011. Architecture and Regulation of the HIV-1 Assembly and Holding Compartment in Macrophages. Journal of virology.

Briggs JA, Riches JD, Glass B, Bartonova V, Zanetti G, Kräusslich HG. 2009. Structure and assembly of immature HIV. Proc Natl Acad Sci U S A. 10627:11090-5.

Dam E, Quercia R, Glass B, Descamps D, Launay O, Duval X, Kräusslich HG, Hance AJ, Clavel F; ANRS 109 Study Group. 2009.
Gag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness loss. PLoS Pathog. 2009 Mar;5(3):e1000345. Epub 2009 Mar 20

Carlson LA, Briggs JA, Glass B, Riches JD, Simon MN, Johnson MC, Müller B, Grünewald K, Kräusslich HG (2008) Three-dimensional analysis of budding sites and released virus suggests a revised model for HIV-1 morphogenesis.Cell Host Microbe 4:592-9.

Welsch S, Keppler OT, Habermann A, Allespach I, Krijnse-Locker J, Kräusslich HG. (2007) HIV-1 buds predominantly at the plasma membrane of primary human macrophages.PLoS Pathog. 3:e36.

Tebit DM, Sangaré L, Makamtse A, Yameogo S, Somlare H, Bado G, Kouldiaty BG, Sathiandee K, Tiba F, Sanou I, Ouédraogo-Traoré R, Zoungrana L, Diallo I, Drabo JY, Kräusslich HG. 2008. HIV drug resistance pattern among HAART-exposed patients with suboptimal virological response in Ouagadougou, Burkina Faso. J Acquir Immune Defic Syndr. 49(1):17-25

Bruegger B, Glass B, Haberkant P, Leibrecht I, Wieland FT, Kraeusslich HG. 2006. The HIV lipidome: a raft with an unusual composition. PNAS 103:2614-2646

Briggs JA, Grünewald K, Glass B, Forster F, Kräusslich HG, Fuller SD. 2006. The Mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 14:15-20.

Sticht J, Humbert M, Findlow S, Bodem J, Müller B, Dietrich U, Werner J and Kräusslich HG. 2005. A peptide inhibitor of HIV-1 assembly in vitro. Nat Struct Mol Biol. 12:671-677

Gottwein E and Kräusslich HG. 2005. Analysis of human immunodeficiency virus type 1 Gag ubiquitination. J Virol. 79:9134-9144

Daecke J, Fackler OT, Dittmar MT, Kräusslich HG. 2005. Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry. J Virol. 79:1581-1594

Bohne J, Wodrich H and Kräusslich HG. 2005. Splicing of human immunodeficiency virus RNA is position-dependent suggesting sequential removal of introns from the 5' end. Nucleic Acids Res. 33:825-837.

Briggs JA, Simon MN, Gross I, Kräusslich HG, Fuller SD, Vogt VM and Johnson MC. 2004. The stoichiometry of Gag protein in HIV-1. Nat Struct Mol Biol. 11:672-675

Müller B, Daecke J, Fackler OT, Dittmar MT, Zentgraf H and Kräusslich HG. 2004.  Construction and characterization of a fluorescently labeled infectious human immunodeficiency virus type 1 derivative.J Virol.78:10803-10813

Tebit DM, Zekeng L, Kaptue L, Gürtler L, Fackler OT, Keppler OT, Herchenröder O, Kräusslich HG. 2004. Construction and characterization of an HIV-1 group O infectious molecular clone and analysis of vpr- and nef-negative derivatives.Virology. 326:329-339.

Briggs, J. A. G., T. Wilk, R. Welker, H.-G. Kräusslich and S. D. Fuller. 2003. The structural organization of authentic HIV-1 and its core. EMBO J. 22: 1707-1715.

Fehrmann, F., M. Jung, R. Zimmermann and H.-G. Kräusslich. 2003. Transport of the Intracisternal A-Type Particle Gag Polyprotein to the Endoplasmic Reticulum is Mediated by Signal Recognition Particle. J. Virol. 77: 6293-6304.

Gottwein, E., J. Bodem, B. Müller, A. Schmechel, H. Zentgraf and H.-G. Kräusslich. 2003. The Mason-Pfizer Monkey Virus PPPY and PSAP Motifs Both Contribute to Virus Release. J. Virol. 77: 9474-9485.

von Schwedler, U., M. Stuchell, B. Müller, D. Ward, H.-Y. Chung, E. Morita, H. E. Wang, T. Davis, G.-P. He, D. M. Cimbora, A. Scott, H.-G. Kräusslich, J. Kaplan, S. G. Morham and W. I. Sundquist. 2003. The Protein Network of HIV Budding. Cell 114: 701-713.

Weber, J., J. R. Mesters, M. Lepšík, J. Prejdová, M. Švec, J. Šponarová, P. Mlcochová, K. Skalicka, K. Stríšovský, T. Uhlíková, M. Soucek, L. Machala, M. Stanková, J. Vondrášek, T. Klimkait, H.-G. Kräusslich, R. Hilgenfeld, and J. Konvalinka. 2002. Unusual binding mode of an HIV-1 protease inhibitor explains its potency against multi-drug-resistant virus strains. J. Mol. Biol. 324: 739-754.

Müller, B., T. Patschinsky, and H.-G. Kräusslich. 2002. The late domain containing protein p6 is the predominant phosphoprotein of HIV-1 particles. J. Virol. 76: 1015-1024.

Wodrich, H., J. Bohne, E. Gumz, R. Welker, and H.-G. Kräusslich. 2001. A new RNA-element located in the coding region of a murine endogenous retrovirus can functionally replace the Rev/Rev responsive element system in human immunodeficiency virus type 1 Gag expression. J. Virol. 75: