pubmed.ncbi.nlm.nih.gov

Unveiling cell surface and type IV secretion proteins responsible for archaeal rudivirus entry - PubMed

  • ️Wed Jan 01 2014

Unveiling cell surface and type IV secretion proteins responsible for archaeal rudivirus entry

Ling Deng et al. J Virol. 2014.

Abstract

Sulfolobus mutants resistant to archaeal lytic virus Sulfolobus islandicus rod-shaped virus 2 (SIRV2) were isolated, and mutations were identified in two gene clusters, cluster sso3138 to sso3141 and cluster sso2386 and sso2387, encoding cell surface and type IV secretion proteins, respectively. The involvement of the mutations in the resistance was confirmed by genetic complementation. Blocking of virus entry into the mutants was demonstrated by the lack of early gene transcription, strongly supporting the idea of a role of the proteins in SIRV2 entry.

Copyright © 2014, American Society for Microbiology. All Rights Reserved.

PubMed Disclaimer

Figures

FIG 1
FIG 1

(A) Growth retardation of S. solfataricus 5E6 upon SIRV2 infection. (B) Resistance of S. solfataricus 5E6R to SIRV2. OD600, optical density at 600 nm.

FIG 2
FIG 2

Analysis of the pyrEF mutants derived from S. solfataricus 5E6. (A) Types and insertion sites of transposons inserted in the pyrEF gene region of different pyrEF mutants. (B) PCR amplification of the pyrEF region from Sens1 to Sens10 and from Res1 to Res10. wt, wild type.

FIG 3
FIG 3

Different mutations in the SIRV2-resistant strains and their stability. (A) Transposon insertions in sso3139 and sso3140. (B) Mutations in sso2386 and sso2387. (C) PCR amplification of the mutation region from different resistant strains.

FIG 4
FIG 4

Cluster sso3138 to sso3141 and cluster sso2386 and sso2387 are involved in SIRV2 entry. (A) Growth retardation of sso3139-complemented Res1 upon SIRV2 infection. Res1 (pEXA), Res1 transformed with expression vector pEXA; Res1 (pEXA3139), Res1 transformed with expression vector pEXA containing sso3139. (B) Growth retardation of sso2386-and-sso2387-complemented Res1B upon SIRV2 infection. Res1B (pEXA), Res1B transformed with expression vector pEXA; Res1B (pEXA2386–2387), Res1B transformed with expression vector pEXA containing sso2386 and sso2387. (C and D) Visualization of SIRV2 DNA replication in Res1 (C) and Res1B (D) transformants infected with SIRV2. Plasmid constructs contained in the transformants are labeled on top of each lane, and the sampling time p.i. is indicated as hours. L and R designate the left and right terminal fragments, respectively, after a double digestion with BamHI and HindIII (see panel E). (E) Schematic presentation of SIRV2 genomic map and the formation of terminal duplex replicative intermediates (2L and 2R), as described previously (12). The locations of the probe (filled rectangle) in the termini are indicated. ITR, inverted terminal repeat. (F) RT-PCR amplification of sso0446 (tfb-1) (left panel) and SIRV2 ORF131a transcript fragments (right panel). “+” and “−” indicate the presence and absence of reverse transcriptase (RT), respectively.

Similar articles

Cited by

References

    1. Prangishvili D, Forterre P, Garrett RA. 2006. Viruses of the Archaea: a unifying view. Nat. Rev. Microbiol. 4:837–848. 10.1038/nrmicro1527 - DOI - PubMed
    1. Pina M, Bize A, Forterre P, Prangishvili D. 2011. The archeoviruses. FEMS Microbiol. Rev. 35:1035–1054. 10.1111/j.1574-6976.2011.00280.x - DOI - PubMed
    1. Peng X, Garrett RA, She Q. 2012. Archaeal viruses–novel, diverse and enigmatic. Sci. China Life Sci. 55:422–433. 10.1007/s11427-012-4325-8 - DOI - PubMed
    1. Erdmann S, Scheele U, Garrett RA. 2011. AAA ATPase p529 of Acidianus two-tailed virus ATV and host receptor recognition. Virology 421:61–66. 10.1016/j.virol.2011.08.029 - DOI - PubMed
    1. Quemin ER, Lucas S, Daum B, Quax TE, Kuhlbrandt W, Forterre P, Albers SV, Prangishvili D, Krupovic M. 2013. First insights into the entry process of hyperthermophilic archaeal viruses. J. Virol. 87:13379–13385. 10.1128/JVI.02742-13 - DOI - PMC - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources