Biochemistry

Secondary metabolites of Hülle cells mediate protection of fungal reproductive and overwintering structures against fungivorous animals

1. Li Liu
2. Christoph Sasse
3. Benedict Dirnberger
4. Oliver Valerius
5. Enikő Fekete-Szücs
6. Rebekka Harting
7. Daniela E Nordzieke
8. Stefanie Pöggeler
9. Petr Karlovsky
10. Jennifer Gerke
11. Gerhard H Braus

• Curated by eLife

  Evaluation Summary:

  Hülle cells, a type of cells formed by fungal species of the genus Aspergillus, are specialized cells that surround the sexual fruiting bodies of ascomycete fungi and are thought to nurse the fruiting bodies during fungal development. In this work, Liu et al. suggest that these cells have a strong ecological impact because they contain specific secondary metabolites that help the fungus to "withstand" the attack by fungivorous animals, like springtails, and also inhibit sexual reproduction of other fungi. This work will likely have a major impact on our view on the development and ecology of fungi as well as on the ecological functions of secondary metabolites.

  (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

Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling

1. Jugal Mohapatra
2. Kyuto Tashiro
3. Ryan L Beckner
4. Jorge Sierra
5. Jessica A Kilgore
6. Noelle S Williams
7. Glen Liszczak

• Curated by eLife

  Evaluation Summary:

  Poly-ADP-ribosylation (poly-ADPr) is a major histone modification that plays critical roles in DNA damage. However careful mechanistic dissection of the role of poly-ADPr has been challenging as the modification is found on multiple proteins and there is heterogeneity in terms of poly-ADP-ribosylation chain length and amino acid location of attachment. The PARP1-dependent semi-synthetic strategy developed by the authors allows generation of nucleosomes with mono ADP ribose and defined lengths of poly-ADPr chains at specific histone serine residues. The utility of this method is clearly demonstrated by the authors' findings that ALC1, a chromatin remodeler that recognizes poly-ADPr is stimulated substantially by the presence of poly-ADPr on H2A and H3.

  (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

Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant

1. Jun Zhang
2. Tianshu Xiao
3. Yongfei Cai
4. Christy L. Lavine
5. Hanqin Peng
6. Haisun Zhu
7. Krishna Anand
8. Pei Tong
9. Avneesh Gautam
10. Megan L. Mayer
11. Richard M. Walsh
12. Sophia Rits-Volloch
13. Duane R. Wesemann
14. Wei Yang
15. Michael S. Seaman
16. Jianming Lu
17. Bing Chen

Reviewed by ScreenIT

A broadly neutralizing biparatopic Nanobody protects mice from lethal challenge with SARS-CoV-2 variants of concern

1. Teresa R. Wagner
2. Daniel Schnepf
3. Julius Beer
4. Karin Klingel
5. Natalia Ruetalo
6. Philipp D. Kaiser
7. Daniel Junker
8. Martina Sauter
9. Bjoern Traenkle
10. Desiree I. Frecot
11. Matthias Becker
12. Nicole Schneiderhan-Marra
13. Annette Ohnemus
14. Martin Schwemmle
15. Michael Schindler
16. Ulrich Rothbauer

Reviewed by ScreenIT

Peptide Scanning of SARS-CoV and SARS-CoV-2 Spike Protein Subunit 1 Reveals Potential Additional Receptor Binding Sites

1. Weilin Lin
2. Jannatul Rafeya
3. Vanessa Roschewitz
4. David Smith
5. Adrian Keller
6. Yixin Zhang

Reviewed by ScreenIT

Framework for rapid comparison of extracellular vesicle isolation methods

1. Dmitry Ter-Ovanesyan
2. Maia Norman
3. Roey Lazarovits
4. Wendy Trieu
5. Ju-Hyun Lee
6. George M Church
7. David R Walt

• Curated by eLife

  Evaluation Summary:

  This manuscript describes a framework for rapidly quantifying relative extracellular vesicle (EV) yield and purity across isolation methods, with a focus on using size exclusion chromatography (SEC) for EV isolation from small volumes of pooled plasma and cerebrospinal fluid (CSF) samples. The authors used single molecule array (Simoa) assays for the quantification of EVs using three tetraspanins (CD9, CD63, and CD81), and report the outcomes of assessing EV yields and purity with respect to albumin by various SEC parameters (Sepharose size, column length, fractions collected). This is the first demonstration of the use of Simoa with three commonly used tetraspanins to measure EVs from small volumes of CSF, of great relevance to human CSF biomarker studies, but these methods could also be applied to compare EV isolation methods from other fluids such as cell culture media.

  (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 and Reviewer #3 agreed to share their names with the authors.)

Reviewed by eLife

Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies)

1. Xudong Wu
2. Tom A. Rapoport

Reviewed by ScreenIT

Native proline-rich motifs exploit sequence context to target actin-remodeling Ena/VASP protein ENAH

1. Theresa Hwang
2. Sara S Parker
3. Samantha M Hill
4. Robert A Grant
5. Meucci W Ilunga
6. Venkatesh Sivaraman
7. Ghassan Mouneimne
8. Amy E Keating

• Curated by eLife

  Evaluation Summary:

  The manuscript introduces a new molecular screen, MassTitr, to screen for long (36-mer) peptides derived from the human proteome that can bind a specific target. The method is demonstrated using the EVH1 domain of the actin-associated ENAH protein as target. About 100 peptides were isolated, and further analysis identified sequence features that contribute to the binding of the EVH1 domain by these peptides. The human proteome contains many short linear motifs of 4-6 residues that are critical for protein-protein interactions. The work here helps to better understand how the sequence surrounding such motifs contributes to protein-protein interactions.

  (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 and Reviewer #2 agreed to share their names with the authors.)

Reviewed by eLife

A distributed residue network permits conformational binding specificity in a conserved family of actin remodelers

1. Theresa Hwang
2. Sara S Parker
3. Samantha M Hill
4. Meucci W Ilunga
5. Robert A Grant
6. Ghassan Mouneimne
7. Amy E Keating

• Curated by eLife

  Evaluation Summary:

  This manuscript describes follow-up studies on a hit from a proteome-wide screen for peptides that can bind to the EVH1 domain of the ENAH protein, one of three highly similar Ena/VASP actin regulators. The hit investigated is from a protein called PCARE, which selectively binds to ENAH but not the other two members of the Ena/VASP family, EVL and VASP. The authors provide a good explanation for how this selectivity is achieved and develop a peptide, PCARE-Dual, that specifically binds ENAH more tightly, setting out the stage for developing potent and selective inhibitors of ENAH activity.

  (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 and Reviewer #2 agreed to share their name with the authors.)

Reviewed by eLife

Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction

1. Naima G Sharaf
2. Mona Shahgholi
3. Esther Kim
4. Jeffrey Y Lai
5. David G VanderVelde
6. Allen T Lee
7. Douglas C Rees

• Curated by eLife

  Evaluation Summary:

  Sharaf and colleagues present an elegant structural and functional analysis of the Neisseria meningitidis ABC transporters MetQ/MetNI illustrating that the substrate binding protein MetQ requires N-terminal lipidation and a substrate (e.g. L-Met and other Met analogs) to stimulate the ATPase, presumably in order to transport the substrate across the inner membrane. This paper will be of broad interest to microbiologists and membrane physiologists who study periplasmic substrate binding proteins and transporter interactions in bacteria.

  (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