Bacteriophage P22 Capsid as a Pluripotent Nanotechnology Tool

被引:10
|
作者
Essus, Victor Alejandro [1 ]
Souza Junior, Getulio Silva e [1 ]
Pereira Nunes, Gabriel Henrique [1 ]
Oliveira, Juliana dos Santos [1 ]
de Faria, Bruna Mafra [2 ]
Romao, Luciana Ferreira [2 ]
Cortines, Juliana Reis [1 ]
机构
[1] Univ Fed Rio de Janeiro, Dept Virol, Lab Virol & Espectrometria Massas LAVEM, Inst Microbiol Paulo Goes, BR-21590902 Rio De Janeiro, Brazil
[2] Univ Fed Rio de Janeiro, Inst Ciencias Biomed, Ave Carlos Chagas Filho,373 CCS,Bl F026, BR-21941590 Rio De Janeiro, Brazil
来源
VIRUSES-BASEL | 2023年 / 15卷 / 02期
关键词
bacteriophage P22; virus-like particles; nanoparticle; protein cage; nanotechnology; VIRUS-LIKE PARTICLES; COAT PROTEIN STRUCTURES; SCAFFOLDING PROTEIN; VIRAL CAPSIDS; ASSEMBLY IDENTIFICATION; CONFORMATIONAL-CHANGES; ENZYME ENCAPSULATION; SALMONELLA PHAGE-P22; MOLECULAR DISPLAY; DNA ENCAPSULATION;
D O I
10.3390/v15020516
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The Salmonella enterica bacteriophage P22 is one of the most promising models for the development of virus-like particle (VLP) nanocages. It possesses an icosahedral T = 7 capsid, assembled by the combination of two structural proteins: the coat protein (gp5) and the scaffold protein (gp8). The P22 capsid has the remarkable capability of undergoing structural transition into three morphologies with differing diameters and wall-pore sizes. These varied morphologies can be explored for the design of nanoplatforms, such as for the development of cargo internalization strategies. The capsid proteic nature allows for the extensive modification of its structure, enabling the addition of non-native structures to alter the VLP properties or confer them to diverse ends. Various molecules were added to the P22 VLP through genetic, chemical, and other means to both the capsid and the scaffold protein, permitting the encapsulation or the presentation of cargo. This allows the particle to be exploited for numerous purposes-for example, as a nanocarrier, nanoreactor, and vaccine model, among other applications. Therefore, the present review intends to give an overview of the literature on this amazing particle.
引用
收藏
页数:39
相关论文
共 50 条
  • [31] INTERACTION OF THE BACTERIOPHAGE P22 ARC REPRESSOR WITH OPERATOR DNA
    VERSHON, AK
    LIAO, SM
    MCCLURE, WR
    SAUER, RT
    JOURNAL OF MOLECULAR BIOLOGY, 1987, 195 (02) : 323 - 331
  • [32] BACTERIOPHAGE P22 MUTANTS THAT ALTER THE SPECIFICITY OF DNA PACKAGING
    JACKSON, EN
    LASKI, F
    ANDRES, C
    JOURNAL OF MOLECULAR BIOLOGY, 1982, 154 (04) : 551 - 563
  • [33] Folding and assembly dynamics of bacteriophage P22 coat protein
    Tuma, R
    Coward, LU
    Kirk, MC
    Barnes, S
    Prevelige, PE
    BIOPHYSICAL JOURNAL, 1999, 76 (01) : A142 - A142
  • [34] GENETIC-STRUCTURE OF THE BACTERIOPHAGE P22 PL OPERON
    SEMERJIAN, AV
    MALLOY, DC
    POTEETE, AR
    JOURNAL OF MOLECULAR BIOLOGY, 1989, 207 (01) : 1 - 13
  • [35] Evaluation of Sample Recovery Efficiency for Bacteriophage P22 on Fomites
    Herzog, Amanda B.
    Pandey, Alok K.
    Reyes-Gastelum, David
    Gerba, Charles P.
    Rose, Joan B.
    Hashsham, Syed A.
    APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2012, 78 (22) : 7915 - 7922
  • [36] CONTRIBUTION OF BACTERIAL RECOMBINATION FUNCTION TO REPLICATION OF BACTERIOPHAGE P22
    YAMAGAMI, H
    YAMAMOTO, N
    JOURNAL OF MOLECULAR BIOLOGY, 1970, 53 (02) : 281 - &
  • [37] Crystallization of the nonameric small terminase subunit of bacteriophage P22
    Roy, Ankoor
    Bhardwaj, Anshul
    Cingolani, Gino
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2011, 67 : 104 - 110
  • [38] INVESTIGATION OF BACTERIOPHAGE P22 DNA-STRUCTURE INSITU
    SKLYADNEVA, VB
    CHEKANOVSKAYA, LA
    GRIGOREV, VB
    TIKHONENKO, TI
    MOLECULAR BIOLOGY, 1981, 15 (01) : 164 - 173
  • [39] Peptide display on functional tailspike protein of bacteriophage P22
    Carbonell, X
    Villaverde, A
    GENE, 1996, 176 (1-2) : 225 - 229
  • [40] Bacteriophage P22 scaffolding protein forms oligomers in solution
    Parker, MH
    Stafford, WF
    Prevelige, PE
    JOURNAL OF MOLECULAR BIOLOGY, 1997, 268 (03) : 655 - 665