Molecular Microbiology最新文献

Protein Homeostasis Impairment Alters Phenotypic Heterogeneity of Biofilm Communities

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-04-17 DOI: 10.1111/mmi.15366

Judith Matavacas, Claes von Wachenfeldt

{"title":"Protein Homeostasis Impairment Alters Phenotypic Heterogeneity of Biofilm Communities","authors":"Judith Matavacas, Claes von Wachenfeldt","doi":"10.1111/mmi.15366","DOIUrl":"https://doi.org/10.1111/mmi.15366","url":null,"abstract":"Biofilms are highly organized, cooperating communities of microorganisms encased in a self-produced extracellular matrix, providing resilience against external stress such as antimicrobial agents and host defenses. A hallmark of biofilms is their phenotypic heterogeneity, which enhances the overall growth and survival of the community. In this study, we demonstrate that removing the dnaK and tig genes encoding the core molecular chaperones DnaK (Hsp70 homolog) and Trigger factor disrupted protein homeostasis in Bacillus subtilis and resulted in the formation of an extremely mucoid biofilm with aberrant architecture, compromised structural integrity, and altered phenotypic heterogeneity. These changes include a large reduction in the motile subpopulation and an overrepresentation of matrix producers and endospores. Overproduction of poly-γ-glutamic acid contributed crucially to the mucoid phenotype and aberrant biofilm architecture. Homeostasis impairment, triggered by elevated temperatures, in wild-type cells led to mucoid and aberrant biofilm phenotypes similar to those observed in strains lacking both dnaK and tig. Our findings show that disruption of protein homeostasis, whether due to the absence of molecular chaperones or because of environmental factors, severely changes biofilm features.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"63 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143841627","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Converting Blastocrithidia Nonstop, a Trypanosomatid With Non-Canonical Genetic Code, Into a Genetically-Tractable Model

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-04-09 DOI: 10.1111/mmi.15365

Arnau Galan, Natalya Kraeva, Kristína Záhonová, Anzhelika Butenko, Alexei Yu Kostygov, Zdeněk Paris, Jiří Pergner, Claretta Bianchi, Fadel Fakih, Andreu Saura, Julius Lukeš, Vyacheslav Yurchenko

引用次数: 0

PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-04-08 DOI: 10.1111/mmi.15363

Momoko Ito, Hideharu Yukitake, Paul D. Veith, Dhana G. Gorasia, Takashi Tominaga, Yuko Sasaki, Eric C. Reynolds, Koji Nakayama, Mariko Naito, Mikio Shoji

{"title":"PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis","authors":"Momoko Ito, Hideharu Yukitake, Paul D. Veith, Dhana G. Gorasia, Takashi Tominaga, Yuko Sasaki, Eric C. Reynolds, Koji Nakayama, Mariko Naito, Mikio Shoji","doi":"10.1111/mmi.15363","DOIUrl":"https://doi.org/10.1111/mmi.15363","url":null,"abstract":"Porphyromonas gingivalis is an important bacterium associated with chronic periodontitis. The type IX secretion system (T9SS) in P. gingivalis secretes conserved C-terminal domain (CTD) containing proteins, which are also called T9SS cargo proteins, including gingipain proteinases, to the cell surface and extracellular milieu. We have shown that gene expression of some T9SS component proteins is regulated by a two-component regulatory system, PorX-PorY, an ECF sigma factor, SigP, and a T9SS cargo protein, PorA. As PorA has its own CTD, PorA is mainly localized as an A-LPS-bound form and PorV-bound form on the cell surface. However, it remains unclear how PorA can activate the PorXY-SigP signaling cascade. In this study, our results revealed that the CTD of PorA can activate the PorXY-SigP signaling cascade via interaction with PorY. It is well known that the canonical role of CTD is to act as a secretion signal for T9SS protein export. In here, we propose a novel concept that the CTD of PorA can play a dual role: as a secretion signal directing the secretion of PorA and as a positive regulator of T9SS gene expression by binding to PorY in the periplasm.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"1 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143797989","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

An Uncharacterized Domain Within the N-Terminal Tail of Histone H3 Regulates the Transcription of FLO1 via Cyc8

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-04-08 DOI: 10.1111/mmi.15362

Ranu Singh, Raghuvir Singh Tomar

{"title":"An Uncharacterized Domain Within the N-Terminal Tail of Histone H3 Regulates the Transcription of FLO1 via Cyc8","authors":"Ranu Singh, Raghuvir Singh Tomar","doi":"10.1111/mmi.15362","DOIUrl":"https://doi.org/10.1111/mmi.15362","url":null,"abstract":"Yeast flocculation relies on cell surface flocculin proteins encoded by the sub-telomeric gene, FLO1. The expression of FLO1 is antagonistically regulated by the Tup1-Cyc8 repressor complex and the Swi-Snf co-activator complexes. The role of hyperacetylated N-terminal amino acid residues of histone H3 and H4 is well established in the transcription of FLO1 and other Tup1-Cyc8 regulated genes. However, sub-domains within the tails of histone H3 and H4 are yet to be identified and the mechanism by which they regulate the FLO1 transcription is completely unexplored. Upon screening of different H3 and H4 N-terminal stretch deletion mutants, we have identified a new region within the N-terminal tail of histone H3, H3Δ(17–24) regulating the transcription of FLO1 and FLO5. This N-terminal truncation mutant showed higher FLO1 and FLO5 expression by 68% and 41% respectively compared to wild-type H3. Further examination showed reduced Cyc8 and nucleosome occupancy in the upstream regulatory region of active flo1 in the H3Δ(17–24) mutant than in H3 wild-type cells. The findings also indicate that Hda1 assists in Cyc8 interaction at the active FLO1 template. Altogether we demonstrate that Tup1-independent interaction of Cyc8 with the active FLO1 gene acts as a transcription limiting factor and that the histone H3 N-terminal 17–24 stretch is essential for this interaction. In the absence of the 17–24 stretch, the Cyc8 restrictive effect is altered, resulting in over-expression of FLO1.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"4 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143798390","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The Power Duo: How the Interplay Between Nucleoid-Associated Proteins and Small Noncoding RNAs Orchestrates the Cellular Regulatory Symphony

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-04-05 DOI: 10.1111/mmi.15359

Sara Moutacharrif, Feth El Zahar Haichar, Sam Meyer, Cecile Ribot, Sylvie Reverchon, William Nasser, Florence Hommais

{"title":"The Power Duo: How the Interplay Between Nucleoid-Associated Proteins and Small Noncoding RNAs Orchestrates the Cellular Regulatory Symphony","authors":"Sara Moutacharrif, Feth El Zahar Haichar, Sam Meyer, Cecile Ribot, Sylvie Reverchon, William Nasser, Florence Hommais","doi":"10.1111/mmi.15359","DOIUrl":"https://doi.org/10.1111/mmi.15359","url":null,"abstract":"In bacteria, the regulation of gene expression involves complex networks that integrate both transcriptional and posttranscriptional mechanisms. At the transcriptional level, nucleoid-associated proteins (NAPs) such as H-NS, HU, Lrp, IHF, Fis and Hfq are key players as they not only compact bacterial DNA but also regulate transcription. Small noncoding RNAs (sRNAs), on the other hand, are known to affect bacterial gene expression posttranscriptionally by base pairing with the target mRNA, but they can also be involved in nucleoid condensation. Interestingly, certain NAPs also influence the function of sRNAs and, conversely, sRNAs themselves can modulate the activity of NAPs, creating a complex bidirectional regulatory network. Here, we summarise the current knowledge of the major NAPs, focusing on the specific role of Hfq. Examples of the regulation of NAPs by sRNAs, the regulation of sRNAs by NAPs and the role of sRNAs in nucleoid structuring are also discussed. This review focuses on the cross-talk between NAPs and sRNAs in an attempt to understand how this interplay works to orchestrate the functioning of the cell.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"20 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143784728","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cellodextrin Metabolism and Phosphotransferase System-Catalyzed Uptake in Enterococcus faecalis.

IF 2.6 2区生物学

Molecular Microbiology Pub Date : 2025-04-01 Epub Date: 2025-02-13 DOI: 10.1111/mmi.15346

Victor Combret, Isabelle Rincé, Ronan Cochelin, Florie Desriac, Cécile Muller, Diane Soussan, Axel Hartke, Josef Deutscher, Nicolas Sauvageot

{"title":"Cellodextrin Metabolism and Phosphotransferase System-Catalyzed Uptake in Enterococcus faecalis.","authors":"Victor Combret, Isabelle Rincé, Ronan Cochelin, Florie Desriac, Cécile Muller, Diane Soussan, Axel Hartke, Josef Deutscher, Nicolas Sauvageot","doi":"10.1111/mmi.15346","DOIUrl":"10.1111/mmi.15346","url":null,"abstract":"Two PTS transporters involved in the uptake of cellobiose and short cellooligosaccharides were identified in Enterococcus faecalis. Genes coding for the different EII proteins are found in a locus composed of three operonic structures expressing two distinct EIIC (CelC1 and CelC2), two identical EIIB (CelB1 and CelB2) and a unique EIIA (CelA1). The EIIA plays a central role in β-glucoside uptake because it is required not only for β-homodiholosides but also for the diheteroside N-acetylglucosamine-L-asparagine. Depending on their size, cellooligosaccharides are preferably transported either by CelC1 (di-saccharides) or by CelC2 (4 glycosidic residues and more), with tri-saccharides being taken up by both EIIC transporters. Moreover, CelA1B2C2 require CelGHI to be functional, three small proteins, the function of which remains unknown. CelA1B1C1 is the main but not exclusive transporter of cellobiose and chitobiose. It is involved in the transport of other β-glucodisaccharides, such as laminaribiose and sophorose. This PTS can be complemented by other transporters highlighting the existence of a network for β-glucoside uptake. This locus is under the control of CelR, a LevR-like transcription activator.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"378-391"},"PeriodicalIF":2.6,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143414629","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Self-Immunity Towards a Novel Competence-Induced Streptococcal Peptidoglycan Hydrolase is Mediated by a Fem-Transferase-Like Protein

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-03-29 DOI: 10.1111/mmi.15361

Marita Torrissen Mårli, Magnus Øverlie Arntzen, Jennie Ann Allred, Anna Teigen Schultheiss, Oddvar Oppegaard, Morten Kjos, Daniel Straume

{"title":"Self-Immunity Towards a Novel Competence-Induced Streptococcal Peptidoglycan Hydrolase is Mediated by a Fem-Transferase-Like Protein","authors":"Marita Torrissen Mårli, Magnus Øverlie Arntzen, Jennie Ann Allred, Anna Teigen Schultheiss, Oddvar Oppegaard, Morten Kjos, Daniel Straume","doi":"10.1111/mmi.15361","DOIUrl":"https://doi.org/10.1111/mmi.15361","url":null,"abstract":"Murein hydrolases (or peptidoglycan hydrolases) play diverse roles in bacteria, from controlled remodeling of the bacterial cell wall to lytic agents. In streptococci, some such hydrolases have been associated with competence-induced fratricide, a process where bacteria kill closely related cells to release DNA that can be taken up during natural transformation. Here, we characterize ScrM, a conserved competence-induced murein hydrolase from Streptococcus dysgalactiae comprising a CHAP domain, an SH3b domain, and an uncharacterized C-terminal domain (CCD). ScrM displayed lytic activity against pyogenic and salivarius group streptococci. Microscopy analysis of fluorescent fusions revealed that ScrM specifically localizes to midcell of sensitive cells, with binding and localization mediated primarily by CCD. Upon competence induction, cells became immune to ScrM due to expression of ScrI, a Fem-transferase-like protein. We show by LC–MS/MS that ScrI incorporates Thr in place of Ala into the interpeptide bridges of peptidoglycan, which in turn prevents ScrM binding to midcell, thereby protecting the cells from self-lysis during competence. ScrM and ScrI are conserved among pyogenic streptococcal pathogens and represent new players in the cell wall biogenesis of these bacteria that may form a platform for the development of novel antimicrobial strategies.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"58 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143734440","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The Plasmodium GRASP Homolog Modulates Liver Stage Development, Subsequent Blood Infection and Virulence in Mice

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-03-26 DOI: 10.1111/mmi.15360

Ella J. Gehrke, Tejram Sahu, Krishna Sathya Manuguri, Christiane Voss, Godfree Mlambo, Beejan Asady, Maryam Saffarian, Julia D. Romano, Isabelle Coppens

{"title":"The Plasmodium GRASP Homolog Modulates Liver Stage Development, Subsequent Blood Infection and Virulence in Mice","authors":"Ella J. Gehrke, Tejram Sahu, Krishna Sathya Manuguri, Christiane Voss, Godfree Mlambo, Beejan Asady, Maryam Saffarian, Julia D. Romano, Isabelle Coppens","doi":"10.1111/mmi.15360","DOIUrl":"https://doi.org/10.1111/mmi.15360","url":null,"abstract":"Conserved across eukaryotic cells, Golgi reassembly and stacking proteins (GRASPs) are peripheral proteins that hold the flat cisternal membranes of the Golgi apparatus into stacks and that also play a role in a process of unconventional protein secretion involving the autophagy machinery. The Golgi in Plasmodium malaria parasites is composed of unstacked cisternae that contain a single GRASP homolog. We previously showed that the initial development of Plasmodium berghei in hepatocytes involves the clearance of micronemes through their sequestration into PbATG8-positive autophagosomes that fuse with the parasite plasma membrane. Here, we examine the involvement of PbGRASP in microneme elimination and extend our studies to assess the importance of GRASP for parasite development in the mammalian host and mosquito vector. GRASP associates with PbATG8 autophagosomes containing micronemes, though PbGRASP-KO parasites can expel micronemes. PbGRASP-KO parasites have no discernable phenotype during mosquito stage development or asexual blood stage growth. PbGRASP-KO liver stages form small schizonts at mid-infection, and then growth resumes. PbGRASP-KO hepatic merozoites egress from the mouse liver and induce higher parasitemia but display delayed and reduced cerebral malaria symptoms. These observations point to a regulatory role for GRASP in controlling parasite proliferation and virulence in mammalian hosts.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"11 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143713593","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Multifaceted Evolution of the PhoPQ Two-Component System in Salmonella enterica Enhanced the Expression of Horizontally Acquired Virulence Genes

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-03-24 DOI: 10.1111/mmi.15355

Luke A. F. Barretto, Casey C. Fowler

{"title":"Multifaceted Evolution of the PhoPQ Two-Component System in Salmonella enterica Enhanced the Expression of Horizontally Acquired Virulence Genes","authors":"Luke A. F. Barretto, Casey C. Fowler","doi":"10.1111/mmi.15355","DOIUrl":"https://doi.org/10.1111/mmi.15355","url":null,"abstract":"For a bacterium to adapt to a new environmental niche, its regulatory networks must evolve to effectively sense and respond to cues within that niche. For bacterial pathogens, which encounter harsh and dynamic host niches that require efficient coordination between detecting host cues and regulating virulence genes, this process is a key aspect of how virulence properties evolve. Here, we investigate how a widely conserved two-component regulatory system (TCS), PhoP/PhoQ (PhoPQ), evolved in Salmonella enterica to adopt a new role as a master regulator of gene expression within its species-specific intracellular niche: the Salmonella-containing vacuole (SCV). By comparing Salmonella PhoPQ with the closely related Escherichia coli PhoPQ ortholog, we demonstrate that optimizing virulence gene expression in Salmonella required a multifaceted evolution of several PhoPQ functional domains and establish that distinct genetic differences and mechanisms enhance virulence gene expression for different inducing cues. Interestingly, we find that the increased activity of the Salmonella PhoPQ system has a much more profound impact on the expression of H-NS-repressed, horizontally acquired virulence genes than on the ancestral members of the PhoP regulon. We observe that the PhoPQ systems of other related bacteria exhibit activity levels similar to the E. coli system, suggesting that the differences we observe are the result of Salmonella-specific adaptations that produced a more active PhoPQ system when encountering SCV conditions. Collectively, this study offers a window into the evolutionary adaptations of a TCS that enable it to assume an expanded regulatory role in a unique environment.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"71 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143695667","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A Soluble Expression Construct of the Isolated Catalytic Domain of Plasmodium falciparum ATP4 Exhibits ATPase Activity Independent of a γ-Phosphate Receiving Aspartate

IF 3.6 2区生物学

Molecular Microbiology Pub Date : 2025-03-17 DOI: 10.1111/mmi.15358

Timo Beyer, Jesko Caliebe, Lara Kähler, Eric Beitz

{"title":"A Soluble Expression Construct of the Isolated Catalytic Domain of Plasmodium falciparum ATP4 Exhibits ATPase Activity Independent of a γ-Phosphate Receiving Aspartate","authors":"Timo Beyer, Jesko Caliebe, Lara Kähler, Eric Beitz","doi":"10.1111/mmi.15358","DOIUrl":"https://doi.org/10.1111/mmi.15358","url":null,"abstract":"The sodium/proton-exchanging ATPase of Plasmodium falciparum malaria parasites, PfATP4, is an emerging drug target. Inhibition results in detrimental cell swelling due to cytosolic accumulation of sodium and alkalization. PfATP4 is a sodium-releasing type II P-type ATPase restricted to apicomplexan parasites. Experimental data on structure–function relationships of the isolated protein are absent. Here, we produced and purified the soluble catalytic domain of PfATP4 and evaluated kinetic properties by in vitro phosphate colorimetry. The protein exhibited Mg2+-dependent ATPase activity at the same order of magnitude as the native cellular PfATP4 and was insensitive to the presence of sodium. AlphaFold 3-based structure and ATP/Mg2+ interaction predictions identified key residues of the nucleotide binding domain (Lys619, Lys652, Arg703). Replacement of the lysines by methionine decreased the enzymatic activity to one quarter. Individual mutation of the putative Mg2+-coordinating Asp865 of the phosphorylation domain was tolerated, while a joint replacement with Asp869 decreased ATPase again to one quarter. Mutation of the putative γ-phosphate receiving Asp451 maintained the rate of Pi release. Our data attribute typical functional roles for P-type ATPases to the basic and acidic residues of the soluble PfATP4 catalytic domain and show that its ATP hydrolysis is independent of phosphorylation of Asp451.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"16 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2025-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143635181","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0