Role of ARP2/3 Complex-Driven Actin Polymerization in RSV Infection

被引:13
|
作者
Paluck, Autumn [1 ]
Osan, Jaspreet [1 ,2 ]
Hollingsworth, Lauren [1 ]
Talukdar, Sattya Narayan [1 ]
Saegh, Ali Al [1 ]
Mehedi, Masfique [1 ]
机构
[1] Univ North Dakota, Sch Med & Hlth Sci, Grand Forks, ND 58202 USA
[2] Weill Cornell Med, Dept Radiat Oncol, New York, NY 10065 USA
来源
PATHOGENS | 2022年 / 11卷 / 01期
关键词
cytoskeleton dynamics; filopodia; ARP2; 3; complex; actin polymerization; cell-to-cell spread; RSV; bronchiolitis; therapeutics; RESPIRATORY SYNCYTIAL VIRUS; NF-KAPPA-B; FILOPODIA FORMATION; COXIELLA-BURNETII; CELLULAR ACTIN; PROTEINS ARP2; RHO GTPASES; CYTOSKELETON; DYNAMICS; MECHANISM;
D O I
10.3390/pathogens11010026
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Respiratory syncytial virus (RSV) is the leading viral agent causing bronchiolitis and pneumonia in children under five years old worldwide. The RSV infection cycle starts with macropinocytosis-based entry into the host airway epithelial cell membrane, followed by virus transcription, replication, assembly, budding, and spread. It is not surprising that the host actin cytoskeleton contributes to different stages of the RSV replication cycle. RSV modulates actin-related protein 2/3 (ARP2/3) complex-driven actin polymerization for a robust filopodia induction on the infected lung epithelial A549 cells, which contributes to the virus's budding, and cell-to-cell spread. Thus, a comprehensive understanding of RSV-induced cytoskeletal modulation and its role in lung pathobiology may identify novel intervention strategies. This review will focus on the role of the ARP2/3 complex in RSV's pathogenesis and possible therapeutic targets to the ARP2/3 complex for RSV.
引用
收藏
页数:12
相关论文
共 50 条
  • [41] Pathway of actin filament branch formation by Arp2/3 complex
    Beltzner, Christopher C.
    Pollard, Thomas D.
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (11) : 7135 - 7144
  • [42] The structural basis of actin filament branching by the Arp2/3 complex
    Rouiller, Isabelle
    Xu, Xiao-Ping
    Amann, Kurt J.
    Egile, Coumaran
    Nickell, Stephan
    Nicastro, Daniela
    Li, Rong
    Pollard, Thomas D.
    Volkmann, Niels
    Hanein, Dorit
    JOURNAL OF CELL BIOLOGY, 2008, 180 (05): : 887 - 895
  • [43] ARP2/3 complex from Acanthamoeba bundles actin filaments
    Kelleher, JF
    Mullins, RD
    Pollard, TD
    MOLECULAR BIOLOGY OF THE CELL, 1996, 7 : 3153 - 3153
  • [44] Characterization of actin nucleating Arp2/3 complex in Trypanosoma brucei
    Pena, J. M.
    Rubotham, J.
    Morales, S.
    Nolan, D.
    Garcia-Salcedo, J. A.
    FEBS JOURNAL, 2012, 279 : 360 - 360
  • [45] The role of nucleotide in Arp2/3 complex function
    Martin, AC
    Welch, M
    Drubin, D
    MOLECULAR BIOLOGY OF THE CELL, 2002, 13 : 317A - 317A
  • [46] Regulation of actin filament assembly by Arp2/3 complex and formins
    Pollard, Thomas D.
    ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 2007, 36 : 451 - 477
  • [47] Regulation of Arp2/3, actin polymerization, and the role of small G proteins in human blood platelets
    Prakash, JM
    Kim, ES
    Bearer, EL
    MOLECULAR BIOLOGY OF THE CELL, 2002, 13 : 317A - 317A
  • [48] Activation of the Arp2/3 complex by the Listeria ActA protein -: ActA binds two actin monomers and three subunits of the Arp2/3 complex
    Zalevsky, J
    Grigorova, I
    Mullins, RD
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (05) : 3468 - 3475
  • [49] Activation of the Arp2/3 complex by N-WASp is required for actin polymerization and contraction in smooth muscle
    Zhang, WW
    Wu, YD
    Du, LP
    Tang, DLD
    Gunst, SJ
    AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2005, 288 (05): : C1145 - C1160
  • [50] Battle of the bulge: the ARP2/3 complex form(in)s an actin phalanx to thwart fungal infection
    Hilleary, Richard
    PLANT CELL, 2021, 33 (09): : 2910 - 2911