Dual ATPase and GTPase activity of the replication-associated protein (Rep) of beak and feather disease virus

Huang, Shr-Wei; Liu, Hao‐Ping; Chen, Jui-Kai; Shien, Y. S.; Wong, Min‐Liang; Wang, Chi-Young

doi:10.1016/j.virusres.2015.12.001

Cited by 7 publications

(5 citation statements)

References 32 publications

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“…These results illustrated that the C-terminal region is important for the functions of MsmK. Walker A and B motifs contribute to the ATPase and GTPase activities of an NTPase, and mutations in the A motif have a relatively remarkable effect on the NTPase activity ( 31 , 32 ). This phenomenon was also observed through the TEM analysis of A_MsmK and B_MsmK.…”

Section: Discussionmentioning

confidence: 88%

“…A number of proteins, such as CvaB of E. coli ( 29 ), SpoIVA of B. subtilis ( 30 ), Rep of beak and feather disease virus ( 31 ), and NS4B of classical swine fever virus ( 32 ), act as nucleoside triphosphatases (NTPases) that hydrolyze ATP and GTP with various levels of activity. Their ATPase and GTPase activities are associated with cell signaling, spore developing, viral replication, or membrane fusion.…”

Section: Discussionmentioning

confidence: 99%

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Streptococcus suis MsmK: Novel Cell Division Protein Interacting with FtsZ and Maintaining Cell Shape

Tan

et al. 2021

mSphere

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Bacteria of different shapes have adopted distinct mechanisms to faithfully coordinate morphogenesis and segregate their chromosomes prior to cell division. Despite recent focuses and advances, the mechanism of cell division in ovococci remains largely unknown. Streptococcus suis, a major zoonotic pathogen that causes problems in human health and in the global swine industry, is an elongated and ellipsoid bacterium that undergoes successive parallel splitting perpendicular to its long axis. Studies on cell cycle processes in this bacterium are limited. Here, we report that MsmK (multiple sugar metabolism protein K), an ATPase that contributes to the transport of multiple carbohydrates, has a novel role as a cell division protein in S. suis. MsmK can display ATPase and GTPase activities, interact with FtsZ via the N terminus of MsmK, and promote the bundling of FtsZ protofilaments in a GTP-dependent manner in vitro. Deletion of the C-terminal region or the Walker A or B motif affects the affinity between MsmK and FtsZ and decreases the ability of MsmK to promote FtsZ protofilament bundling. MsmK can form a complex with FtsZ in vivo, and its absence is not lethal but results in long chains and short, occasionally anuclear daughter cells. Superresolution microscopy revealed that the lack of MsmK in cells leads to normal septal peptidoglycan walls in mother cells but disturbed cell elongation and peripheral peptidoglycan synthesis. In summary, MsmK is a novel cell division protein that maintains cell shape and is involved in the synthesis of the peripheral cell wall. IMPORTANCE Bacterial cell division is a highly ordered process regulated in time and space and is a potential target for the development of antimicrobial drugs. Bacteria of distinct shapes depend on different cell division mechanisms, but the mechanisms used by ovococci remain largely unknown. Here, we focused on the zoonotic pathogen Streptococcus suis and identified a novel cell division protein named MsmK, which acts as an ATPase of the ATP-binding cassette-type carbohydrate transport system. MsmK has GTPase and ATPase activities. In vitro protein assays showed that MsmK interacts with FtsZ and promotes FtsZ protofilament bundling that relies on GTP. Superresolution microscopy revealed that MsmK maintains cell shape and is involved in peripheral peptidoglycan synthesis. Knowledge of the multiple functions of MsmK may broaden our understanding of known cell division processes. Further studies in this area will elucidate how bacteria can faithfully and continually multiply in a constantly changing environment.

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Section: Discussionmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Streptococcus suis MsmK: Novel Cell Division Protein Interacting with FtsZ and Maintaining Cell Shape

Tan

et al. 2021

mSphere

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“…The endonuclease domain of Rep is located at the N-terminus and is responsible for recognition of the origin of replication motif in the viral genome sequence, as well as being responsible for the endonuclease activity that enables nicking of the circular DNA and initiation of RCR (62). Recombinant Rep protein exhibits dual ATPase and GTPase activity (31). Rep proteins typically contain a helicase domain for DNA unwinding (33), and while helicase activity of Rep has been demonstrated for two different geminiviruses (a family of viruses distinct from circoviruses yet with similar circular ssDNA genomes and replication strategies) ( 16), solid evidence remains to be established for helicase activity in circoviruses.…”

Section: Rep Proteinmentioning

confidence: 99%

“…A consensus ATP/ GTP-binding motif was detected in geminiviruses and is seemingly essential for viral genome replication (8). A study demonstrated that the dual ATPase and GTPase activity of the C-terminal domain of the BFDV Rep is regulated by Walker A and B motifs typical of ATP-binding proteins, as well as a novel GYDG motif that is encoded between them (31).…”

Section: Rep Proteinmentioning

confidence: 99%

“…Rep protein has thus been suggested to bind with Cap and to be cotranslocated across the nuclear envelope. The ATPase and GTPase activity of the BFDV Rep was also upregulated in the presence of Cap protein, which suggests that the interaction between the Rep and Cap proteins may lead to conformational and/or functional change in the Rep protein (31). However, since no structural data are available for these complexes, a detailed understanding of this interaction, and possible biological function is limited.…”

Section: Rep Proteinmentioning

confidence: 99%

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Structural Perspectives of Beak and Feather Disease Virus and Porcine Circovirus Proteins

et al. 2021

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Circoviruses represent a rapidly expanding group of viruses that infect both vertebrate and invertebrate hosts. Members are responsible for diseases of veterinary and economic importance, including postweaning multisystemic wasting syndrome in pigs, and beak and feather disease (BFD) in birds. These viruses are associated with lymphoid depletion and immunosuppressive conditions in infected animals leading to systemic illness. Circoviruses are small nonenveloped DNA viruses containing a single-stranded circular genome, encoding two major proteins: the capsid-associated protein (Cap), comprising the entirety of the viral capsid, and the replication-associated protein (Rep). Cap is the only protein component of the virion and plays crucial roles throughout the virus replication cycle, including viral attachment, cell entry, genome uncoating, and packaging of newly formed viral particles. Rep mediates recognition of replication origin motifs in the viral genome sequence and is responsible for endonuclease activity enabling nicking of the circular DNA and initiation of rolling-circle replication (RCR). Porcine circovirus 2 (PCV2) was the first circovirus capsid structure to be solved at atomic resolution using X-ray crystallography. The structure revealed an assembly comprising 60 monomeric subunits to form virus-like particles. Each Cap monomer harbors a canonical viral jelly roll domain composed of two, four-stranded antiparallel b-sheets. Crystal structures of two distinct macromolecular assemblies from BFD virus Cap were also resolved at high resolution. In these structures, the exposure of the N-terminal arginine-rich motif, responsible for DNA binding and nuclear localization is reversed. Additional structural investigations have also elucidated a PCV2 type-specific neutralizing epitope, and interaction between the PCV2 capsid and polymers such as heparin. In this review, we provide a snapshot of the structural and functional aspects of circovirus proteins.

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Development of an antigen-capture ELISA for beak and feather disease virus

Huang

Chan

et al. 2017

Arch Virol

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Psittacine beak and feather disease (PBFD) is characterised by degenerative feather, feather dystrophy, and beak deformity. Sometimes acute forms can lead to fatal cases in nestlings. The worldwide distribution of this disease affects numerous species of parrots with an average prevalence of 40%, including in Taiwan. The pathogen of PBFD is beak and feather disease virus (BFDV), which is a single-stranded circular DNA virus, circovirus. To date, hemagglutination and PCR assays have been routinely used to detect this virus. In this study, both the replication-associated protein (Rep) and the structural capsid protein (Cap) were expressed and then used as antigens for the production of monoclonal antibodies. Conserved epitopes recognised by the anti-Cap and anti-Rep monoclonal antibodies were determined to be NFEDYRI and LSALKKM, respectively. Clinical samples collected from different species of parrots were tested by hemagglutination, PCR, and anti-Cap antigen-capture ELISA assays and the positive rates were the same at 49%. Thus, this anti-Cap antigen-capture ELISA is able to be used for the rapid identification of BFDV-infected birds in a non-invasive manner.

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Dual ATPase and GTPase activity of the replication-associated protein (Rep) of beak and feather disease virus

Cited by 7 publications

References 32 publications

Streptococcus suis MsmK: Novel Cell Division Protein Interacting with FtsZ and Maintaining Cell Shape

Streptococcus suis MsmK: Novel Cell Division Protein Interacting with FtsZ and Maintaining Cell Shape

Structural Perspectives of Beak and Feather Disease Virus and Porcine Circovirus Proteins

Development of an antigen-capture ELISA for beak and feather disease virus

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