Biophysics

Fluorescence signatures of SARS-CoV-2 spike S1 proteins and a human ACE-2: excitation-emission maps and fluorescence lifetimes

1. Jonas Grzesiak
2. Lea Fellner
3. Karin Grünewald
4. Christoph Kölbl
5. Arne Walter
6. Reinhold Horlacher
7. Frank Duschek

Reviewed by ScreenIT

Landscape-Based Mutational Sensitivity Cartography and Network Community Analysis of the SARS-CoV-2 Spike Protein Structures: Quantifying Functional Effects of the Circulating D614G Variant

1. Gennady M. Verkhivker
2. Steve Agajanian
3. Deniz Yasar Oztas
4. Grace Gupta

Reviewed by ScreenIT

Presence of a SARS-COV-2 protein enhances Amyloid Formation of Serum Amyloid A

1. Asis K. Jana
2. Augustus B. Greenwood
3. Ulrich H. E. Hansmann

Reviewed by ScreenIT

Molecular rationale for SARS-CoV-2 spike circulating mutations able to escape bamlanivimab and etesevimab monoclonal antibodies

1. Erik Laurini
2. Domenico Marson
3. Suzana Aulic
4. Alice Fermeglia
5. Sabrina Pricl

Reviewed by ScreenIT

Structural intermediates observed only in intact Escherichia coli indicate a mechanism for TonB-dependent transport

1. Thushani D Nilaweera
2. David A Nyenhuis
3. David S Cafiso

• Curated by eLife

  Evaluation Summary:

  The manuscript endeavors to explain the mechanism of action of the gram-negative bacterial outer membrane TonB-dependent transporter BtuB, which acquires vitamin B12 from the external environment. The authors use electron paramagnetic resonance spectroscopy to monitor the proximity of different parts of this protein to one another during the binding of B12 directly in the E. coli outer membrane. This manuscript will be of interest to those who study the biophysics of membrane transporters and stresses the importance of studying membrane proteins in their native environment.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #2 and Reviewer #3 agreed to share their names with the authors.)

Reviewed by eLife

Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53

1. Kaushik Inamdar
2. Feng-Ching Tsai
3. Rayane Dibsy
4. Aurore de Poret
5. John Manzi
6. Peggy Merida
7. Remi Muller
8. Pekka Lappalainen
9. Philippe Roingeard
10. Johnson Mak
11. Patricia Bassereau
12. Cyril Favard
13. Delphine Muriaux

• Curated by eLife

  Evaluation Summary:

  This manuscript combines cell biology, biochemistry, and quantitative biophysics to understand a new host cell factor, the human I-BAR domain protein IRSp53, promotes HIV type 1 (HIV-1) assembly and release. Since this new factor is a protein involved in the generation and sensing of negative membrane curvature, this manuscript will be of interest not only for retrovirologists and virologists in general but also for membrane biologists and biophysicists.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1, Reviewer #2 and Reviewer #3 agreed to share their names with the authors.)

Reviewed by eLife

in silico Assessment of Antibody Drug Resistance to Bamlanivimab of SARS-CoV-2 Variant B.1.617

1. Leili Zhang
2. Tien Huynh
3. Binquan Luan

Reviewed by ScreenIT

The crystal structure of bromide-bound GtACR1 reveals a pre-activated state in the transmembrane anion tunnel

1. Hai Li
2. Chia-Ying Huang
3. Elena G Govorunova
4. Oleg A Sineshchekov
5. Adrian Yi
6. Kenneth J Rothschild
7. Meitian Wang
8. Lei Zheng
9. John L Spudich

• Curated by eLife

  Evaluation Summary:

  This manuscript reports a significant contribution towards an improved mechanistic understanding of light gated anion channels. The studies, which use the recently established method of in meso in situ serial data collection (IMISX), provide a basis for optimizing the anion channelrhodopsin GtACR1 from the alga Guillardia theta as a neuron-inhibiting optogenetics tool. The work will be of interest to anyone using optogenetics for functional studies. The reviewers had a few comments regarding technical aspects of the work.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. The reviewers remained anonymous to the authors)

Reviewed by eLife

Energy landscape of the SARS-CoV-2 reveals extensive conformational heterogeneity

1. Ghoncheh Mashayekhi
2. John Vant
3. Abhigna Polavarapu
4. Abbas Ourmazd
5. Abhishek Singharoy

Reviewed by ScreenIT

Handling of intracellular K+ determines voltage dependence of plasmalemmal monoamine transporter function

1. Shreyas Bhat
2. Marco Niello
3. Klaus Schicker
4. Christian Pifl
5. Harald H Sitte
6. Michael Freissmuth
7. Walter Sandtner

• Curated by eLife

  Evaluation Summary:

  This paper will be of interest to scientists interested in mechanistic studies of ion-coupled transporters. The authors demonstrate that dopamine, catecholamine and serotonin transporters - albeit structurally very similar - differ in the number of transport substrates and they define the underlying functional basis of this difference using a range of sophisticated techniques. This is an extremely nice and interesting study. providing new tools and new insights into an important class of transporter. Since many drugs that block one of the transporters also modify the two others, the paper may help to define pharmaceutical approaches that specifically block only one of them and that might allow for a better treatment of psychiatric diseases. The data analysis is rigorous and the conclusions are justified by the data, but the paper should be made more "user friendly" so that a wider audience could appreciate it better.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #3 agreed to share their name with the authors.)

Reviewed by eLife