Microbiology

Virological characteristics of the SARS-CoV-2 Omicron BA.2 subvariants, including BA.4 and BA.5

1. Izumi Kimura
2. Daichi Yamasoba
3. Tomokazu Tamura
4. Naganori Nao
5. Tateki Suzuki
6. Yoshitaka Oda
7. Shuya Mitoma
8. Jumpei Ito
9. Hesham Nasser
10. Jiri Zahradnik
11. Keiya Uriu
12. Shigeru Fujita
13. Yusuke Kosugi
14. Lei Wang
15. Masumi Tsuda
16. Mai Kishimoto
17. Hayato Ito
18. Rigel Suzuki
19. Ryo Shimizu
20. MST Monira Begum
21. Kumiko Yoshimatsu
22. Kanako Terakado Kimura
23. Jiei Sasaki
24. Kaori Sasaki-Tabata
25. Yuki Yamamoto
26. Tetsuharu Nagamoto
27. Jun Kanamune
28. Kouji Kobiyama
29. Hiroyuki Asakura
30. Mami Nagashima
31. Kenji Sadamasu
32. Kazuhisa Yoshimura
33. Kotaro Shirakawa
34. Akifumi Takaori-Kondo
35. Jin Kuramochi
36. Gideon Schreiber
37. Ken J. Ishii
38. Takao Hashiguchi
39. Terumasa Ikeda
40. Akatsuki Saito
41. Takasuke Fukuhara
42. Shinya Tanaka
43. Keita Matsuno
44. Kei Sato

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Distinct antigenic properties of the SARS-CoV-2 Omicron lineages BA.4 and BA.5

1. Brian J. Willett
2. Ashwini Kurshan
3. Nazia Thakur
4. Joseph Newman
5. Maria Manali
6. Grace Tyson
7. Nicola Logan
8. Pablo R. Murcia
9. Luke B. Snell
10. Jonathan D. Edgeworth
11. Jie Zhou
12. Ksenia Sukhova
13. Gayatri Amirthalingam
14. Kevin Brown
15. Bryan Charleston
16. Michael H. Malim
17. Emma C. Thomson
18. Wendy S. Barclay
19. Dalan Bailey
20. Katie J. Doores
21. Thomas P. Peacock

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Intranasal vaccination induced cross-protective secretory IgA antibodies against SARS-CoV-2 variants with reducing the potential risk of lung eosinophilic immunopathology

1. Takuya Hemmi
2. Akira Ainai
3. Takao Hashiguchi
4. Minoru Tobiume
5. Takayuki Kanno
6. Naoko Iwata-Yoshikawa
7. Shun Iida
8. Yuko Sato
9. Sho Miyamoto
10. Akira Ueno
11. Kaori Sano
12. Shinji Saito
13. Nozomi Shiwa-Sudo
14. Noriyo Nagata
15. Koji Tamura
16. Ryosuke Suzuki
17. Hideki Hasegawa
18. Tadaki Suzuki

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Host-directed therapy with 2-deoxy-D-glucose inhibits human rhinoviruses, endemic coronaviruses, and SARS-CoV-2

1. Laxmikant Wali
2. Michael Karbiener
3. Scharon Chou
4. Vitalii Kovtunyk
5. Adam Adonyi
6. Irene Gösler
7. Ximena Contreras
8. Delyana Stoeva
9. Dieter Blaas
10. Johannes Stöckl
11. Thomas R. Kreil
12. Guido A. Gualdoni
13. Anna-Dorothea Gorki

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Further antibody escape by Omicron BA.4 and BA.5 from vaccine and BA.1 serum

1. Aekkachai Tuekprakhon
2. Jiandong Huo
3. Rungtiwa Nutalai
4. Aiste Dijokaite-Guraliuc
5. Daming Zhou
6. Helen M. Ginn
7. Muneeswaran Selvaraj
8. Chang Liu
9. Alexander J. Mentzer
10. Piyada Supasa
11. Helen M.E. Duyvesteyn
12. Raksha Das
13. Donal Skelly
14. Thomas G. Ritter
15. Ali Amini
16. Sagida Bibi
17. Sandra Adele
18. Sile Ann Johnson
19. Bede Constantinides
20. Hermione Webster
21. Nigel Temperton
22. Paul Klenerman
23. Eleanor Barnes
24. Susanna J. Dunachie
25. Derrick Crook
26. Andrew J Pollard
27. Teresa Lambe
28. Philip Goulder
29. OPTIC consortium
30. ISARIC4C consortium
31. Elizabeth E. Fry
32. Juthathip Mongkolsapaya
33. Jingshan Ren
34. David I. Stuart
35. Gavin R Screaton

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Using a reverse genetics system to generate recombinant SARS-CoV-2 expressing robust levels of reporter genes

1. Chengjin Ye
2. Luis Martinez-Sobrido

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Omicron breakthrough infections in vaccinated or previously infected hamsters

1. Jie Zhou
2. Ksenia Sukhova
3. Thomas P. Peacock
4. Paul F. McKay
5. Jonathan C. Brown
6. Rebecca Frise
7. Laury Baillon
8. Maya Moshe
9. Ruthiran Kugathasan
10. Robin J. Shattock
11. Wendy S. Barclay

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SARS-CoV-2 ORF1ab ^A1061S potentiate autoreactive T cell responses via epitope mimicry: an explanation to hepatitis of unknown cause

1. Yu Wang
2. Yuexing Liu

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The Spike-Stabilizing D614G Mutation Interacts with S1/S2 Cleavage Site Mutations To Promote the Infectious Potential of SARS-CoV-2 Variants

1. Stacy Gellenoncourt
2. Nell Saunders
3. Rémy Robinot
4. Lucas Auguste
5. Maaran Michael Rajah
6. Jérôme Kervevan
7. Raphaël Jeger-Madiot
8. Isabelle Staropoli
9. Cyril Planchais
10. Hugo Mouquet
11. Julian Buchrieser
12. Olivier Schwartz
13. Lisa A. Chakrabarti

Reviewed by ScreenIT

Investigating the composition and recruitment of the mycobacterial ImuA′–ImuB–DnaE2 mutasome

1. Sophia Gessner
2. Zela Alexandria-Mae Martin
3. Michael A Reiche
4. Joana A Santos
5. Ryan Dinkele
6. Atondaho Ramudzuli
7. Neeraj Dhar
8. Timothy J de Wet
9. Saber Anoosheh
10. Dirk M Lang
11. Jesse Aaron
12. Teng-Leong Chew
13. Jennifer Herrmann
14. Rolf Müller
15. John D McKinney
16. Roger Woodgate
17. Valerie Mizrahi
18. Česlovas Venclovas
19. Meindert H Lamers
20. Digby F Warner

• Curated by eLife

  Evaluation Summary:

  Drug resistance in a problem in the control of many infections, including Mycobacterium tuberculosis. In mycobacteria, an error prone DNA polymerase facilitates DNA damage induced mutagenesis to increase the rate of generation of drug resistant strains. The previously identified mutasome components ImuA', ImuB, and DnaE2 and essential for DNA-damage induced mutagenesis. In this manuscript, the authors test their previously proposed model that ImuB interacts with the DnaN DNA polymerase III β clamp to recruit DnaE2. This is of interest to a broad audience interested in microbiology, antibiotic resistance, and genome stability.

  (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