TASK DEFINITION: In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.
PROBLEM: Cryptosporidiosis is one of the most common zoonosis worldwide, causing intestinal infection to both humans and livestock. The purpose of this study was to assess whether the level of anti-C. parvum IgG antibodies transferred through colostrum from dams to newborn calves impacts the susceptibility to cryptosporidiosis. A number of 50 dams and their healthy newborns were included in the study. Colostrum samples were collected within 12 h after birth and anti-C. parvum IgG antibody levels were determined by single radial immunodiffusion. The health condition of the newborns was daily monitored, and fecal samples were collected at first diarrheic episode of a calf. In all dams, the anti-C. parvum IgG antibody concentration in colostrum varied between 570 and 4070 mg/dl; in dams who gave birth to calves with diarrhea and were C. parvum-positive, the antibody concentration in colostrum varied between 680 and 3680 mg/dl (Table 1 ). The point-biserial correlation showed a negative correlation between the levels of anti-C. parvum antibodies and manifestation of clinical cryptosporidiosis (r=-0.425). Our findings highlight the importance of IgG levels in colostrum received by neonatal calves during their first day of life for prevention of C. parvum infection.

SOLUTION: Importance of colostrum IgG antibodies level for prevention of infection with Cryptosporidium parvum in neonatal dairy calves

PROBLEM: A new species of parvovirus, tentatively named human bocavirus 4 (HBoV4), was genetically characterized. Among 641 feces samples obtained from children and adults, the most commonly detected bocavirus species were, in descending order, HBoV2, HBoV3, HBoV4, and HBoV1, with an HBoV2 prevalence of 21% and 26% in Nigerian and Tunisian children, respectively. HBoV3 or HBoV4 species were found in 12 of 192 patients with non-polio acute flaccid paralysis in Tunisia and Nigeria and 0 of 96 healthy Tunisian contacts (P p ). Evidence of extensive recombination at the NP1 and VP1 gene boundary between and within bocavirus .01 species was found. The high degree of genetic diversity seen among the human bocaviruses found in feces specimens, relative to the highly homogeneous HBoV1, suggest that this worldwide-distributed respiratory pathogen may have recently evolved from an enteric bocavirus after acquiring an expanded tropism favoring the respiratory tract. Elucidating the possible role of the newly identified enteric bocaviruses in human diseases, including acute flaccid paralysis and diarrhea, will require further epidemiological studies. Parvoviruses are small, non-lipid-enveloped, environmentally resistant viral particles with single-stranded linear DNA genomes that frequently infect animals through the fecal-oral route [1] . Parvoviruses can cause numerous symptoms in animals, including enteritis, panleukopenia, hepatitis, erythrocyte aplasia, and cerebellar ataxia [1]. Efficacious vaccines against animal parvovirus infections are widely employed [2] [3] [4] . Following the identification of the human parvovirus

SOLUTION: Human Bocaviruses Are Highly Diverse, Dispersed, Recombination Prone, and Prevalent in Enteric Infections

PROBLEM: The nonstructural polyproteins of Sindbis virus are processed by a virus-encoded proteinase which is located in the C-terminal domain of nsP2. Here we have performed a mutagenic analysis to identify the active site residues of this proteinase. Substitution of other amino acids for either Cys-481 or His-558 completely abolished proteolytic processing of Sindbis virus polyproteins in vitro. Substitutions within this domain for a second cysteine conserved among alphaviruses, for four other conserved histidines, or for a conserved serine did not affect the activity of the enzyme. These results suggest that nsP2 is a papain-like proteinase whose catalytic dyad is composed of Cys-481 and His-558. Since an asparagine residue has been implicated in the active site of papain, we changed the four conserved asparagine residues in the C-terminal half of nsP2 and found that all could be substituted without total loss of activity. Among papain-like proteinases, the residue following the catalytic histidine is alanine or glycine in the plant and animal enzymes, and the presence of Trp-559 in alphaviruses is unusual. A mutant enzyme containing Ala-559 was completely inactive, implying that Trp-559 is essential for a functional proteinase. All of these mutations were introduced into a full-length clone of Sindbis virus from which infectious RNA could be transcribed in vitro, and the effects of these changes on viability were tested. In all cases it was found that mutations which abolished proteolytic activity were lethal, whether or not these mutations were in the catalytic residues, indicating that proteolysis of the nonstructural polyprotein is essential for Sindbis replication. 0 1992 Academic press, hc.

SOLUTION:
Identification of the Active Site Residues in the nsP2 Proteinase of Sindbis Virus