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PubMed2000

Host-range barrier of influenza A viruses.

Ample evidence suggests that all influenza viruses in mammals were probably derived from those in wild waterfowl at some time. In addition to those already established in mammals, the viruses have been transmitted to both mammals and to poultry from wild waterfowl and caused outbreaks in recent years. Experimentally, however, the viruses from one species of animals do not grow efficiently in other species. For example, human influenza viruses do not replicate in ducks or in horses, indicating their host range restriction. This paper reviews current knowledge on the host-range restriction of influenza viruses, focusing on the role of the hemagglutinin (HA).

Animals↗
PubMed1991

Regulation of plaque size and host range by a vaccinia virus gene related to complement system proteins.

A vaccinia virus variant, LC16m8, and its parental Lister (Elstree) strain (LO) were employed to identify the viral gene(s) responsible for plaque size and host range: the large-plaque-forming LO strain but not the small-plaque-forming LC16m8 strain can actively proliferate in Vero (YTV) cells. Previously, we suggested that some particular gene(s) present in the HindIII D fragment of LO DNA was responsible for these biological activities. In the present experiment, the mapping of the putative gene was done by introducing various subfragments of the HindIII D fragment of LO DNA into the gene of LC16m8 strain and screening of the resultant virus variants for the capability of forming large plaques or of proliferating well in Vero cells. The results indicated that an open reading frame (called ps/hr gene) in LO HindIII D fragment was responsible for either plaque size or host range. This gene encoded a polypeptide of 317 amino acids related to the regulators of complement activation (RCA) gene family of mammals. Thus, the present genetic analysis provided direct evidence for a previously unrecognized function of RCA-related proteins encoded by the virus.

Amino Acid Sequence↗
PubMed1975

Virion trascriptase activity differences in host range mutants of vesicular stomatitis virus.

Three types of conditional lethal mutant were isolated from wild-type vesicular stomatitis virus, New Jersey serotype, after mutagenization by 5-fluorouracil: (i) conventional temperature-sensitive (ts) mutants, which form plaques at 31 C but not at 39 C; (ii) conventional host range mutants (hr CE), which grow in BHK but not in secondary chicken embryo cells; and (iii) temperature-dependent host range mutants (td CE), which form plaques both at 31 and 39 C on BHK cells but only at 31 C on chicken embryo cells. To determine whether the mutation in hr CE and td CE mutants affected the virion-associated RNA transcriptase, this enzyme was assayed in vitro at 31 and 39 C, and the results were compared with those obtained for the wild-type virus. The RNA trascriptase activity of hr CE mutants did not appear to be affected by the mutation. The td CE mutants fall into two classes: those that synthesized RNA at 39 C similar to the wild-type virus and those that did not. One mutant of the latter category, td CE 3, had heat-sensitive transcriptase regardless of whether it was grown in BHK or chicken embryo cells. A revertant to the wild-type phenotype isolated from this mutant had regained the ability to synthesize RNA at 39 C. These results strongly suggest that a polypeptide that is either the transcriptase itself or part of the transcriptase complex was made temperature sensitive by the mutation in the second class of td CE mutants. The inhibition of the transcriptase activity of the mutant td CE 3 was fully reversible by lowering the temperature of incubation from 39 to 31 C, and both inhibition and reactivation appeared to be instantaneous.

Animals↗
PubMed1973

Murine C-type RNA virus from spontaneous neoplasms: in vitro host range and oncogenic potential.

Strain BALB/c mice harbor at least two host range variants of marine leukemia virus. One variant, which is host-cell tropic, is the predominant isolate from neoplastic tissues and produced lymphoreticular neoplasms when injected into BALB/c newborn mice. A second variant, whicht is isolated throughout life, grows poorly in host embryonic cells in culture and was not associated with lymphoreticular neoplasm induction when injected into newborn BALB/c mice.

Animals↗
PubMed1983

Host range differences among xenotropic type C retroviruses isolated from mouse kidney cell cultures.

By co-cultivation procedures, infectious xenotropic type C viruses have been recovered from kidney cells of several strains of mice. They have host-range patterns which place them into separate subgroups. In cells cultivated from one NZB kidney, two biologically different xenotropic type C retroviruses were found. One, X-NZB/K-1, infects and replicates well in human and mink fibroblast cells but does not induce foci in mink S + L - cells with good efficiency. The other, X-NZB/K-2, infects and replicates well in mink but not human fibroblast cells, and induces foci readily in mink S + L - cells. Cross-infection studies indicate that these viruses, classified as xenotropic by host range and envelope properties, are genetically stable.

Animals↗
PubMed1992

The NS and capsid genes determine the host range of porcine parvovirus.

Porcine parvovirus is an autonomous parvovirus which normally infects pigs and multiplies in porcine cells in vitro. In this report, we describe the properties of a variant designated P2, which has extended its host range to include canine cells. The variant was able to produce cytopathic effects (CPE) in canine cells, unlike the prototype NADL-2 strain. The variant also produced higher viral antigen and infectivity titers in canine cells than the NADL-2 strain, whereas both strains produced CPE and similar titers in porcine cells. Generation of recombinant plasmids between the P2 variant DNA and an infectious clone of NADL-2, and analysis of the properties of the virus stocks produced from these recombinant plasmids, indicated that two changes were necessary for this extension in the host range. One change was located in the nonstructural protein coding region and the other in the capsid coding region.

Amino Acid Sequence↗
PubMed1983

Isolation and characterization of mink cell focus-inducing murine leukemia viruses with xenotropic host range from mouse strain SL.

A new type of mink cell focus-inducing virus was persistently isolated from the leukemic tissues of SL mice. In contrast to the dual tropic mink cell focus-inducing viruses reported to date, the new virus has the host range of the xenotropic murine leukemia virus. Analysis of RNase T(1) fingerprints of genomic RNAs suggested that the mink cell focus-inducing virus with the xenotropic host range isolated from SL mice is a recombinant virus deriving from xenotropic murine leukemia virus.

Animals↗
PubMed1980

Mutant and recombinant avian retroviruses with extended host range.

Avian retroviruses of subgroups B and D efficiently infect chicken (C/E) but not turkey (T/BD) cells. We describe here three variants of subgroup B and D viruses that infect both cell types equally well. One of these viruses, NTRE-4, was a recombinant between transformation-defective Prague (Pr) strain Rous sarcoma virus (RSV) subgroup B and the endogenous virus RAV-0; the second, SR-DE-1, was a recombinant between Schmidt-Ruppin RSV subgroup D and defective endogenous virus information. T1 oligonucleotide fingerprint analysis of the genomes of these two viruses showed only a small alteration in the portion of the env gene responsible for subgroup specificity, as indicated by the presence of a single subgroup E oligonucleotide in an otherwise purely subgroup B or D gene. The third virus, hrBO1Pr-B, was a variant of Pr-RSV-B that did not appear to be a recombinant and whose altered host range we attribute to mutation. Analysis of the host range of all three viruses by infection of selectively resistant cells and by interference testing indicates that all use the subgroup B receptor on chicken cells and the subgroup E receptor on turkey cells. These viruses may be analogous to the polytropic recombinant viruses recently found to be associated with leukemia in some strains of mice.

Animals↗
PubMed1997

[Host range of influenza viruses and their receptor binding specificities].

Host-range of influenza viruses are established by many factors in nature such as the quantitative, qualitative aspects of the viral receptor, the permissive and non permissive states of host-cell condition, and also the antibody and inhibitor pressure present in the host. Influenza virus hemagglutinin recognizes specific sialyl-sugar chains of the host cell membranes. In this paper, the structure and function of sialyl-sugar chains as influenza virus receptors are described in relation to the variation of influenza viruses and the molecular evolution of influenza virus hemagglutinin.

Hemagglutinin Glycoproteins, Influenza Virus↗
PubMed1998

In vitro and in vivo host range of Anticarsia gemmatalis multiple nuclear polyhedrosis virus.

A clone of the wild type (wt) Anticarsia gemmatalis multiple nuclear polyhedrosis virus AgMNPV, derived from a geographical isolate (Hondrina, Brazil) and designated AgMNPV-CL4-3A1, was used to determine the host range of this virus in six established lepidopteran cell lines: Anticarsia gemmatalis (BCIRL-AG-AM1), Helicoverpa zea (BCIRL-HZ-AM1), Heliothis virescens (BCIRL-HV-AM1), Helicoverpa armigera (BCIRL-HA-AM1), Trichoplusia ni (TN-CL1), Bombyx mori (BMN), and a coleopteran cell line Anthonomus grandis (BRL-AG-1). In addition, the in vivo host range of this clone was also assayed in larvae of Helicoverpa zea, Heliothis virescens, Trichoplusia ni, and the homologous species Anticarsia gemmatalis by probit analysis. On the basis of temporal studies of TCID50 values, BCIRL-HV-AM1 cells gave the highest extracellular virus (ECV) titer (9.7 x 10(6) TCID50/ml) followed by BCIRL-HA-AM1 cells (8.3 x 10(5) TCID50/ml) and BCIRL-AG-AM1 cells (3.2 x 10(5) TCID50/ml). In addition, a low ECV titer of 1.37 x 10(3) TCID50/ml was detected from TN-CL1 cells 96 h postinoculation, while BRL-AG-1, BMN, and BCIRL-HZ-AM1 cells were nonpermissive to AgMNPV-CL4-3A1 on the basis of TCID50 results. AgMNPV-CL4-3A1 and the wild type AgMNPV had similar restriction profiles that were different from wild type AcMNPV. The LC50 values were 96.9, 564.6, 733.3, and 1.1 x 10(4) occlusion bodies/cm2 of diet for A. gemmatalis, Helicoverpa zea, Heliothis virescens, and T. ni, respectively.

Animals↗
PubMed1995

The pre-S domain of the large viral envelope protein determines host range in avian hepatitis B viruses.

In addition to their well-recognized hepatotropism, all hepatitis B viruses (HBVs) display marked species specificity, growing poorly or not at all in species other than those closely related to their natural hosts. We have examined the molecular basis for this narrow host range, using duck HBV (DHBV) and heron HBV (HHBV) as a model system. HHBV virions will not infect ducks in vivo and infect cultured duck hepatocytes extremely inefficiently in vitro. Mutant HHBV genomes lacking all viral envelope proteins (HHBV env-) can be complemented in trans with DHBV envelope proteins; the resulting pseudotyped virions can efficiently infect duck hepatocytes. Further complementation analysis reveals that of the two viral surface proteins (L and S), it is the L protein that determines host range. Pseudotyping of HHBV env- with DHBV/HHBV chimeric envelope proteins reveals that replacement of as few as 69 amino acids of the pre-S domain of the HHBV L protein by their DHBV counterparts is sufficient to permit infection of duck hepatocytes. These studies indicate that the species-specificity of hepadnaviral infection is determined at the level of virus entry and is governed by the pre-S domain of the viral L protein.

Amino Acid Sequence↗
PubMed2024

Shedding light on Klebsiella pneumoniae virulence: Engineering of broad host range bioluminescence reporter vectors for transcriptional analysis in drug resistant pathogens.

In this work, we report the construction of four bacterial luciferase-based promoter probe vectors with an expanded set of selectable markers, designed to facilitate their use in antibiotic-resistant bacteria. These vectors contain the low-copy-number, broad-host-range pBBR origin of replication and an origin of transfer, allowing efficient conjugative transformation into various bacterial genera. The broad host range origin also enables their use in bacterial strains that harbor other plasmids, as the pBBR origin is compatible with a wide variety of other plasmid replication systems. The utility of these vectors was demonstrated by quantifying capsule gene expression in both classical and hypervirulent Klebsiella pneumoniae strains lacking tolC, which encodes the outer membrane pore protein for tripartite transport systems. Our results revealed that the tolC mutation reduced capsule gene expression, highlighting a critical role for tolC in K. pneumoniae pathobiology and the utility of bioluminescence for studying gene expression in real time. These new vectors provide a flexible platform for circumventing antibiotic resistance phenotypes and studying gene expression across diverse bacterial species, including strains containing additional plasmids.

Klebsiella pneumoniae↗
PubMed1997

Canine parvovirus host range is determined by the specific conformation of an additional region of the capsid.

We analyzed a region of the capsid of canine parvovirus (CPV) which determines the ability of the virus to infect canine cells. This region is distinct from those previously shown to determine the canine host range differences between CPV and feline panleukopenia virus. It lies on a ridge of the threefold spike of the capsid and is comprised of five interacting loops from three capsid protein monomers. We analyzed 12 mutants of CPV which contained amino acid changes in two adjacent loops exposed on the surface of this region. Nine mutants infected and grew in feline cells but were restricted in replication in one or the other of two canine cell lines tested. Three other mutants whose genomes contain mutations which affect one probable interchain bond were nonviable and could not be propagated in either canine or feline cells, although the VP1 and VP2 proteins from those mutants produced empty capsids when expressed from a plasmid vector. Although wild-type and mutant capsids bound to canine and feline cells in similar amounts, infection or viral DNA replication was greatly reduced after inoculation of canine cells with most of the mutants. The viral genomes of two host range-restricted mutants and two nonviable mutants replicated to wild-type levels in both feline and canine cells upon transfection with plasmid clones. The capsids of wild-type CPV and two mutants were similar in susceptibility to heat inactivation, but one of those mutants and one other were more stable against urea denaturation. Most mutations in this structural region altered the ability of monoclonal antibodies to recognize epitopes within a major neutralizing antigenic site, and that site could be subdivided into a number of distinct epitopes. These results argue that a specific structure of this region is required for CPV to retain its canine host range.

Animals↗
PubMed2005

A wide host-range metagenomic library from a waste water treatment plant yields a novel alcohol/aldehyde dehydrogenase.

Using DNA obtained from the metagenome of an anaerobic digestor in a waste water treatment plant, we constructed a gene library cloned in the wide host-range cosmid pLAFR3. One cosmid enabled Rhizobium leguminosarum to grow on ethanol as sole carbon and energy source, this being due to the presence of a gene, termed adhEMeta. The AdhEMeta protein most closely resembles the AdhE alcohol dehydrogenase of Clostridium acetobutylicum, where it catalyses the formation of ethanol and butanol in a two-step reductive process. However, cloned adhEMeta did not confer ethanol utilization ability to Escherichia coli or to Pseudomonas aeruginosa, even though it was transcribed in both these hosts. Further, cell-free extracts of E. coli and R. leguminosarum containing cloned adhEMeta had butanol and ethanol dehydrogenase activities when assayed in vitro. In contrast to the well-studied AdhE proteins of C. acetobutylicum and E. coli, the enzyme specified by adhEMeta is not inactivated by oxygen and it enables alcohol to be catabolized. Cloned adhEMeta did, however, confer one phenotype to E. coli. AdhE- mutants of E. coli fail to ferment glucose and introduction of adhEMeta restored the growth of such mutants when grown under fermentative conditions. These observations show that the use of wide host-range vectors enhances the efficacy with which metagenomic libraries can be screened for genes that confer novel functions.

Alcohol Dehydrogenase↗
PubMed2006

Host range restriction and pathogenicity in the context of influenza pandemic.

Influenza A viruses cause pandemics at random intervals. Pandemics are caused by viruses that contain a hemagglutinin (HA) surface glycoprotein to which human populations are immunologically naive. Such an HA can be introduced into the human population through reassortment between human and avian virus strains or through the direct transfer of an avian influenza virus to humans. The factors that determine the interspecies transmission and pathogenicity of influenza viruses are still poorly understood; however, the HA protein plays an important role in overcoming the interspecies barrier and in virulence in avian influenza viruses. Recently, the RNA polymerase (PB2) protein has also been recognized as a critical factor in host range restriction, while the nonstructural (NS1) protein affects the initial host immune responses. We summarize current knowledge of viral factors that determine host range restriction and pathogenicity of influenza A viruses.

Amino Acid Sequence↗
PubMed2005

Vaccinia virus K1L protein mediates host-range function in RK-13 cells via ankyrin repeat and may interact with a cellular GTPase-activating protein.

The K1L protein of vaccinia virus is required for its growth in certain cell lines (RK-13 and human). The cowpox host-range protein CP77 has been shown to complement K1L function in RK-13 cells, despite a lack of homology between the two proteins except for ankyrin repeats. We investigated the role of ankyrin repeats of K1L protein in RK-13 cells. The growth of a recombinant vaccinia virus, with K1L gene mutated in the most conserved ankyrin repeat, was severely impaired. Infection with the mutant virus caused shutdown of cellular and viral protein synthesis early in infection. We also investigated the interaction of K1L protein with cellular proteins and found that K1L interacts with the rabbit homologue of human ACAP2, a GTPase-activating protein with ankyrin repeats. Our result suggests the importance of ankyrin repeat for host-range function of K1L in RK-13 cells and identifies ACAP2 as a cellular protein, which may be interacting with K1L.

Amino Acid Sequence↗
PubMed1984

Molecular gentic analysis of the trfB and korB region of broad host range plasmid RK2.

A 3.2 kb region of the broad host range IncP plasmid RK2 (indistinguishable from RP1, RP4, R68 and R18) anticlockwise from the EcoRI site may be separated phenotypically into three loci. The trfB/korA/korD locus both complements a temperature-sensitive maintenance mutation and suppresses the deleterious effects of the loci kilA and kilD; the incC locus expresses incompatibility towards complete RK2-like replicons, and the korB locus suppresses the host lethal effect the kilB locus. Transcriptional fusions of the galK gene to various segments of this region revealed that all three loci are transcribed anticlockwise from a common promoter. A weak secondary promoter may also contribute to the expression of korB. Analysis of the sizes of the polypeptides produced from these segments led to the identification of two cistrons, the first encoding a polypeptide of 38 kDal associated with incC function and the second a polypeptide of 49 kDal associated with korB activity. The trfB/korA/korD activities are associated with a polypeptide of 14kDal which may be an N-terminal fragment of the incC-associated polypeptide.

Chromosome Mapping↗
PubMed1994

Autophosphorylation is required for high kinase activity and efficient transformation ability of proteins encoded by host range alleles of v-src.

pp60v-src is a nonreceptor protein tyrosine kinase that can transform both chicken and rodent fibroblasts. The src homology 2 (SH2) domain of this protein serves a critical role in the regulation of protein tyrosine kinase activity. The host range proteins pp60v-src-L, which contains a deletion of a highly conserved residue (Phe-172) in the SH2 domain, and pp60v-src-PPP, which contains a change from a Leu to a Phe at amino acid 186 in the SH2 domain, transform chicken but not rat cells and have slightly reduced kinase activity measured in vitro. The data presented here show that these altered proteins require autophosphorylation on Tyr-416 for high kinase activity and transforming ability. In the absence of autophosphorylation, there is a further decrease of at least threefold in in vitro kinase activity relative to the phosphorylated host range parental protein, no morphological transformation, a reduction in anchorage independent growth, and no disruption of the actin cytoskeleton. In addition, these SH2 mutations abolish the ability of the SH2 domain to bind a phosphorylated peptide that corresponds to the autophosphorylation site of pp60src. Thus, like mutant alleles of c-src encoding transformation competent proteins, and unlike v-src, transformation by pp60v-src-F172 delta and pp60v-src-L186F is dependent on phosphorylation of Y-416 for high kinase activity and transformation ability. The dependence of transformation on phosphotyrosine is not a reflection of an intramolecular interaction between the autophosphorylation site and the SH2 domains since purified SH2 domains are incapable of binding phosphorylated autophosphorylation site peptides in vitro.

Alleles↗